On the evolution of coenzyme biosynthesis

An Earth-system perspective of the global nitrogen cycle

Gruber, N., & Galloway, J. N. (2008) · Nature · doi:10.1038/nature06592 · Cited by 3,595 · see citing works

Origin of life: The RNA world

Gilbert, W. (1986) · Nature · doi:10.1038/319618a0 · Cited by 2,721 · see citing works

Hydrogenases

Lubitz, W., Ogata, H., Rüdiger, O., & Reijerse, E. J. (2014) · Chemical Reviews · doi:10.1021/cr4005814 · Cited by 2,067 · see citing works

Iron-sulfur clusters: nature's modular, multipurpose structures

Beinert, H., Holm, R. H., & Münck, E. (1997) · Science · doi:10.1126/science.277.5326.653 · Cited by 1,944 · see citing works

Mechanism of Molybdenum Nitrogenase

Burgess, B. K., & Lowe, D. J. (1996) · Chemical Reviews · doi:10.1021/cr950055x · Cited by 1,854 · see citing works

The P450 Superfamily: Update on New Sequences, Gene Mapping, Accession Numbers, Early Trivial Names of Enzymes, and Nomenclature

Nelson, D. R., Kamataki, T., Waxman, D. J., Guengerich, F. P., Estabrook, R. W., Feyereisen, R., Gonzalez, F. J., Coon, M. J., GUNSALUS, I. C., Gotoh, O., et al. (1993) · DNA and Cell Biology · doi:10.1089/dna.1993.12.1 · Cited by 1,637 · see citing works

Occurrence, Classification, and Biological Function of Hydrogenases: An Overview

Vignais, P. M., & Billoud, B. (2007) · Chemical Reviews · doi:10.1021/cr050196r · Cited by 1,571 · see citing works

The Shikimate Pathway and Aromatic Amino Acid Biosynthesis in Plants

Maeda, H. A., & Dudareva, N. (2012) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042811-105439 · Cited by 1,568 · see citing works

Distribution of isoprenoid quinone structural types in bacteria and their taxonomic implication

Collins, M. D., & Jones, D. A. (1981) · Microbiological Reviews · doi:10.1128/mr.45.2.316-354.1981 · Cited by 1,457 · see citing works

Structure, function, and formation of biological iron-sulfur clusters

Johnson, D. C., Dean, D. R., Smith, A. D., & Johnson, M. K. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133518 · Cited by 1,438 · see citing works

Acetogenesis and the Wood–Ljungdahl pathway of CO2 fixation

Ragsdale, S. W., & Pierce, E. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2008.08.012 · Cited by 1,337 · see citing works

Biochemistry of methanogenesis: a tribute to Marjory Stephenson:1998 Marjory Stephenson Prize Lecture

Thauer, R. K. (1998) · Microbiology · doi:10.1099/00221287-144-9-2377 · Cited by 1,112 · see citing works

The antiquity of RNA-based evolution.

Joyce, G. F. (2002) · Nature · doi:10.1038/418214a · Cited by 1,070 · see citing works

NAD+ metabolism in health and disease

Belenky, P. A., Bogan, K. L., & Brenner, C. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.11.006 · Cited by 983 · see citing works

Pyridoxal Phosphate Enzymes: Mechanistic, Structural, and Evolutionary Considerations

Eliot, A. C., & Kirsch, J. F. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074021 · Cited by 955 · see citing works

The Natural History of Nitrogen Fixation

Raymond, J., Siefert, J. L., Staples, C. R., & Blankenship, R. E. (2004) · Molecular Biology and Evolution · doi:10.1093/molbev/msh047 · Cited by 887 · see citing works

Structure–function relationships of alternative nitrogenases

Eady, R. R. (1996) · Chemical Reviews · doi:10.1021/cr950057h · Cited by 877 · see citing works

RadicalS-Adenosylmethionine Enzymes

Broderick, J. B., Duffus, B. R., Duschene, K. S., & Shepard, E. M. (2014) · Chemical Reviews · doi:10.1021/cr4004709 · Cited by 827 · see citing works

The emergence of life from iron monosulphide bubbles at a submarine hydrothermal redox and pH front

RUSSELL, M. J., & HALL, A. J. (1997) · Journal of the Geological Society · doi:10.1144/gsjgs.154.3.0377 · Cited by 822 · see citing works

Iron-sulfur proteins: ancient structures, still full of surprises

Beinert, H. (2000) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750050002 · Cited by 667 · see citing works

Structure and function of DNA photolyase

Sancar, A. (1994) · Biochemistry · doi:10.1021/bi00167a001 · Cited by 663 · see citing works

The V-type H+ ATPase: molecular structure and function,physiological roles and regulation

Beyenbach, K. W., & Wieczorek, H. (2006) · Journal of Experimental Biology · doi:10.1242/jeb.02014 · Cited by 630 · see citing works

An evolving view of methane metabolism in the Archaea

Evans, P. N., Boyd, J. A., Leu, A. O., Woodcroft, B. J., Parks, D. H., Hugenholtz, P., & Tyson, G. W. (2019) · Nature Reviews Microbiology · doi:10.1038/s41579-018-0136-7 · Cited by 614 · see citing works

Review of Poly (ADP-ribose) Polymerase (PARP) Mechanisms of Action and Rationale for Targeting in Cancer and Other Diseases

Morales, J. C., Li, L.-S., Fattah, F. J., Dong, Y., Bey, E. A., Patel, M., Gao, J., & Boothman, D. A. (2013) · Critical Reviews in Eukaryotic Gene Expression · doi:10.1615/critreveukaryotgeneexpr.2013006875 · Cited by 613 · see citing works

COBALAMIN (COENZYME B 12 ): Synthesis and Biological Significance

Roth, J., Lawrence, J., & Bobik, T. (1996) · Annual Review of Microbiology · doi:10.1146/annurev.micro.50.1.137 · Cited by 566 · see citing works

The origins of the RNA world

Robertson, M. P., & Joyce, G. F. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a003608 · Cited by 556 · see citing works

The Shikimate Pathway: Early Steps in the Biosynthesis of Aromatic Compounds.

Herrmann, K. M. (1995) · The Plant Cell · doi:10.1105/tpc.7.7.907 · Cited by 496 · see citing works

UNUSUAL COENZYMES OF METHANOGENESIS

DiMarco, A. A., Bobik, T. A., & WOLFE, R. S. (1990) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.59.070190.002035 · Cited by 496 · see citing works

The biosynthesis of adenosylcobalamin (vitamin B12)

Warren, M. J., Raux, E., Schubert, H., & Escalante‐Semerena, J. C. (2002) · Natural Product Reports · doi:10.1039/b108967f · Cited by 484 · see citing works

Vitamin B 12 , folate, and the methionine remethylation cycle—biochemistry, pathways, and regulation

Froese, D. S., Fowler, B., & Baumgartner, M. R. (2019) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12009 · Cited by 479 · see citing works

Microbial production of vitamin B12: a review and future perspectives

Fang, H., Kang, J., & Zhang, D. (2017) · Microbial Cell Factories · doi:10.1186/s12934-017-0631-y · Cited by 466 · see citing works

On the Mechanism of the Formose Reaction

Breslow, R. (1959) · Tetrahedron Letters · doi:10.1016/s0040-4039(01)99487-0 · Cited by 456 · see citing works

S-Adenosyl-l-methionine: Beyond the universal methyl group donor

Roje, S. (2006) · Phytochemistry · doi:10.1016/j.phytochem.2006.04.019 · Cited by 439 · see citing works

Methanogens: biochemical background and biotechnological applications

Enzmann, F., Mayer, F., Rother, M., & Holtmann, D. (2018) · AMB Express · doi:10.1186/s13568-017-0531-x · Cited by 439 · see citing works

The DNA (cytosine-5) methyltransferases

Kumar, S., Cheng, X., Klimašauskas, S., Mi, S., Pósfai, J., Roberts, R. J., & Wilson, G. G. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.1.1 · Cited by 429 · see citing works

S‐Adenosyl‐Methionine‐Dependent Methyltransferases: Highly Versatile Enzymes in Biocatalysis, Biosynthesis and Other Biotechnological Applications

Struck, A., Thompson, M. L., Wong, L. S., & Micklefield, J. (2012) · ChemBioChem · doi:10.1002/cbic.201200556 · Cited by 428 · see citing works

Hydrogenases from Methanogenic Archaea, Nickel, a Novel Cofactor, and H2 Storage

Thauer, R. K., Kaster, A., Goenrich, M., Schick, M. B., Hiromoto, T., & Shima, S. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.030508.152103 · Cited by 419 · see citing works

Universality in intermediary metabolism

Smith, E., & Morowitz, H. J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404922101 · Cited by 408 · see citing works

Biosynthesis of Pantothenic Acid and Coenzyme A

Leonardi, R., & Jackowski, S. (2007) · EcoSal Plus · doi:10.1128/ecosalplus.3.6.3.4 · Cited by 404 · see citing works

The Origin of Life—Out of the Blue

Sutherland, J. D. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201506585 · Cited by 401 · see citing works

Enzymology of the Wood–Ljungdahl Pathway of Acetogenesis

Ragsdale, S. W. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1419.015 · Cited by 384 · see citing works

Structure and function of enzymes in heme biosynthesis

Layer, G., Reichelt, J., Jahn, D., & Heinz, D. W. (2010) · Protein Science · doi:10.1002/pro.405 · Cited by 357 · see citing works

Fe-S Cluster Assembly Pathways in Bacteria

Ayala-Castro, C. N., Saini, A. K., & Outten, F. W. (2008) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00034-07 · Cited by 343 · see citing works

Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product

Dailey, H. A., Dailey, T. A., Gerdes, S., Jahn, D., Jahn, M., O'Brian, M. R., & Warren, M. J. (2017) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00048-16 · Cited by 340 · see citing works

The origin of intermediary metabolism

Morowitz, H. J., Kostelnik, J. D., Yang, J. J., & Cody, G. D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.110153997 · Cited by 338 · see citing works

Enzymology of one-carbon metabolism in methanogenic pathways

Ferry, J. G. (1999) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.1999.tb00390.x · Cited by 316 · see citing works

Biosynthesis of Vitamin B2 (Riboflavin)

Bacher, A., Eberhardt, S., Fischer, M. J., Kis, K., & Richter, G. (2000) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.20.1.153 · Cited by 316 · see citing works

The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli

Schwartz, C. J., Djaman, O., Imlay, J. A., & Kiley, P. J. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.160261497 · Cited by 301 · see citing works

The folic acid biosynthesis pathway in bacteria: evaluation of potential for antibacterial drug discovery

Bermingham, A., & Derrick, J. P. (2002) · BioEssays · doi:10.1002/bies.10114 · Cited by 295 · see citing works

Structure of the photolyase-like domain of cryptochrome 1 from Arabidopsis thaliana

Brautigam, C. A., Smith, B. S., Ma, Z., Palnitkar, M., Tomchick, D. R., Machius, M., & Deisenhofer, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404851101 · Cited by 293 · see citing works

Thiamin biosynthesis in prokaryotes

Begley, T. P., Downs, D. M., Ealick, S. E., McLafferty, F. W., van Loon, A. P. G. M., Taylor, S. V., Campobasso, N., Chiu, H., Kinsland, C. L., Reddick, J. J., et al. (1999) · Archives of Microbiology · doi:10.1007/s002030050713 · Cited by 292 · see citing works

Bioenergetics and anaerobic respiratory chains of aceticlastic methanogens

Welte, C. U., & Deppenmeier, U. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.12.002 · Cited by 287 · see citing works

Cobalamin-Dependent Methyltransferases

Matthews, R. G. (2001) · Accounts of Chemical Research · doi:10.1021/ar0000051 · Cited by 287 · see citing works

From Genetic Footprinting to Antimicrobial Drug Targets: Examples in Cofactor Biosynthetic Pathways

Gerdes, S., Scholle, M. D., D’Souza, M., Bernal, A., Baev, M. V., Farrell, M., Kurnasov, O. V., Daugherty, M. D., Mseeh, F., Polanuyer, B. M., et al. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.16.4555-4572.2002 · Cited by 282 · see citing works

The Biosynthesis of Folic Acid

Brown, G. M. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93957-8 · Cited by 275 · see citing works

The Molybdenum Cofactor

Mendel, R. R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.455311 · Cited by 272 · see citing works

ADP-Ribosylation, a Multifaceted Posttranslational Modification Involved in the Control of Cell Physiology in Health and Disease

Lüscher, B., Bütepage, M., Eckei, L., Krieg, S., Verheugd, P., & Shilton, B. H. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00122 · Cited by 258 · see citing works

NAD(P) synthesis and pyridine nucleotide cycling in plants and their potential importance in stress conditions

Noctor, G. (2006) · Journal of Experimental Botany · doi:10.1093/jxb/erj202 · Cited by 253 · see citing works

Systems Biology of Metabolism

Nielsen, J. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044757 · Cited by 252 · see citing works

An Alternative Menaquinone Biosynthetic Pathway Operating in Microorganisms

Hiratsuka, T., Furihata, K., Ishikawa, J., Yamashita, H., Itoh, N., Seto, H., & Dairi, T. (2008) · Science · doi:10.1126/science.1160446 · Cited by 252 · see citing works

Radical-Mediated Enzymatic Methylation: A Tale of Two SAMS

Zhang, Q., van der Donk, W. A., & Liu, W. (2011) · Accounts of Chemical Research · doi:10.1021/ar200202c · Cited by 249 · see citing works

Insights into [FeFe]-Hydrogenase Structure, Mechanism, and Maturation

Mulder, D. W., Shepard, E. M., Meuser, J. E., Joshi, N., King, P. W., Posewitz, M. C., Broderick, J. B., & Peters, J. W. (2011) · Structure · doi:10.1016/j.str.2011.06.008 · Cited by 249 · see citing works

Vitamin B6 biosynthesis in higher plants

Tambasco-Studart, M., Titiz, O., Raschle, T., Forster, G., Amrhein, N., & Fitzpatrick, T. B. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506228102 · Cited by 248 · see citing works

Naturally occurring 5-deazaflavin coenzymes: biological redox roles

Walsh, C. T. (1986) · Accounts of Chemical Research · doi:10.1021/ar00127a004 · Cited by 240 · see citing works

Mechanistic concepts of iron-sulfur protein biogenesis in Biology

Braymer, J. J., Freibert, S., Rakwalska‐Bange, M., & Lill, R. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118863 · Cited by 235 · see citing works

The biosynthesis of coenzyme a in bacteria

Begley, T. P., Kinsland, C. L., & Strauss, E. (2001) · Vitamins and hormones · doi:10.1016/s0083-6729(01)61005-7 · Cited by 233 · see citing works

Microbial NAD Metabolism: Lessons from Comparative Genomics

Gazzaniga, F., Stebbins, R., Chang, S. Z., McPeek, M. A., & Brenner, C. (2009) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00042-08 · Cited by 230 · see citing works

Trinuclear Cuboidal and Heterometallic Cubane-Type Iron–Sulfur Clusters: New Structural and Reactivity Themes in Chemistry and Biology

Holm, R. H. (1992) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(08)60061-6 · Cited by 228 · see citing works

Remnants of an Ancient Metabolism without Phosphate

Goldford, J. E., Hartman, H., Smith, T. F., & Segrè, D. (2017) · Cell · doi:10.1016/j.cell.2017.02.001 · Cited by 226 · see citing works

Two independent routes of de novo vitamin B6 biosynthesis: not that different after all

Fitzpatrick, T. B., Amrhein, N., Kappes, B., Macheroux, P., Tews, I., & Raschle, T. (2007) · Biochemical Journal · doi:10.1042/bj20070765 · Cited by 221 · see citing works

Radical Mechanisms of Enzymatic Catalysis

Frey, P. A. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.121 · Cited by 218 · see citing works

Biotin synthesis begins by hijacking the fatty acid synthetic pathway

Lin, S., Hanson, R. E., & Cronan, J. E. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.420 · Cited by 216 · see citing works

The Origin and Nature of Life on Earth: The Emergence of the Fourth Geosphere

Smith, E., & Morowitz, H. J. (2016) · doi:10.1017/cbo9781316348772 · Cited by 215 · see citing works

Crystal Structure of Histidine Ammonia-Lyase Revealing a Novel Polypeptide Modification as the Catalytic Electrophile,

Schwede, T. F., Rétey, J., & Schulz, G. E. (1999) · Biochemistry · doi:10.1021/bi982929q · Cited by 214 · see citing works

Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum

Raux, E., Schubert, H., & Warren, M. J. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000670 · Cited by 211 · see citing works

Biosynthesis of flavocoenzymes

Fischer, M. J., & Bacher, A. (2005) · Natural Product Reports · doi:10.1039/b210142b · Cited by 189 · see citing works

Physiology, Biochemistry, and Applications of F 420 - and F o -Dependent Redox Reactions

Greening, C., Ahmed, F. H., Mohamed, A. E., Lee, B. M., Pandey, G., Warden, A. C., Scott, C. S., Oakeshott, J. G., Taylor, M. C., & Jackson, C. J. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00070-15 · Cited by 188 · see citing works

DNA-binding by Ig-fold proteins.

Rudolph, M. J., & Gergen, J. P. (2001) · Nature Structural Biology · doi:10.1038/87531 · Cited by 173 · see citing works

Molybdenum enzymes, their maturation and molybdenum cofactor biosynthesis in Escherichia coli

Iobbi‐Nivol, C., & Leimkühler, S. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.11.007 · Cited by 170 · see citing works

Iron–sulfur cluster biosynthesis

Bandyopadhyay, S., Chandramouli, K., & Johnson, M. K. (2008) · Biochemical Society Transactions · doi:10.1042/bst0361112 · Cited by 169 · see citing works

The evolution of A‐, F‐, and V‐type ATP synthases and ATPases: reversals in function and changes in the H⁺/ATP coupling ratio

Cross, R. L., & Müller, V. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.08.065 · Cited by 168 · see citing works

Synthetic connectivity, emergence, and self-regeneration in the network of prebiotic chemistry

Wołos, A., Roszak, R., Żądło‐Dobrowolska, A., Beker, W., Mikulak-Klucznik, B., Spólnik, G., Dygas, M., Szymkuć, S., & Grzybowski, B. A. (2020) · Science · doi:10.1126/science.aaw1955 · Cited by 166 · see citing works

Molybdenum cofactor biosynthesis and deficiency

Schwarz, G. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5269-y · Cited by 163 · see citing works

Horizontal gene transfer constrains the timing of methanogen evolution

Wolfe, J. M., & Fournier, G. P. (2018) · Nature Ecology & Evolution · doi:10.1038/s41559-018-0513-7 · Cited by 160 · see citing works

[FeFe]‐Hydrogenase Cyanide Ligands Derived From S ‐Adenosylmethionine‐Dependent Cleavage of Tyrosine

Driesener, R. C., Challand, M. R., McGlynn, S. E., Shepard, E. M., Boyd, E. S., Broderick, J. B., Peters, J. W., & Roach, P. L. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.200907047 · Cited by 159 · see citing works

Closing in on complete pathways of biotin biosynthesis

Lin, S., & Cronan, J. E. (2011) · Molecular BioSystems · doi:10.1039/c1mb05022b · Cited by 158 · see citing works

UV-light-driven prebiotic synthesis of iron-sulfur clusters

Bonfio, C., Valer, L., Scintilla, S., Shah, S., Evans, D. J., Jin, L., Szostak, J. W., Sasselov, D. D., Sutherland, J. D., & Mansy, S. S. (2017) · Nature Chemistry · doi:10.1038/nchem.2817 · Cited by 158 · see citing works

Assembly of Lipoic Acid on Its Cognate Enzymes: an Extraordinary and Essential Biosynthetic Pathway

Cronan, J. E. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00073-15 · Cited by 155 · see citing works

Biosynthesis of biotin and lipoic acid

Marquet, A., Bui, B. T. S., & Florentin, D. (2001) · Vitamins and hormones · doi:10.1016/s0083-6729(01)61002-1 · Cited by 151 · see citing works

The semi-phosphorylative Entner–Doudoroff pathway in hyperthermophilic archaea: a re-evaluation

Ahmed, H., Ettema, T. J. G., Tjaden, B., Geerling, A. C. M., John van der, O. O. S. T., & Siebers, B. (2005) · Biochemical Journal · doi:10.1042/bj20041711 · Cited by 146 · see citing works

The biosynthesis of nicotinamide adenine dinucleotides in bacteria

Begley, T. P., Kinsland, C. L., Mehl, R. A., Osterman, A. L., & Dorrestein, P. C. (2001) · Vitamins and hormones · doi:10.1016/s0083-6729(01)61003-3 · Cited by 143 · see citing works

Vitamin B12: How the Problem of Its Biosynthesis Was Solved

Blanche, F., Cameron, B., Crouzet, J., Debüssche, L., Thibaut, D., Vuilhorgne, M., Leeper, F. J., & Battersby, A. R. (1995) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199503831 · Cited by 142 · see citing works

Mechanistic Investigations of Lipoic Acid Biosynthesis in Escherichia coli : Both Sulfur Atoms in Lipoic Acid are Contributed by the Same Lipoyl Synthase Polypeptide

Cicchillo, R. M., & Booker, S. J. (2005) · Journal of the American Chemical Society · doi:10.1021/ja042428u · Cited by 139 · see citing works

Tetrapyrrole assembly and modification into the ligands of biologically functional cofactors

Warren, M. J., & Scott, A. I. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90304-t · Cited by 135 · see citing works

A Possible Prebiotic Formation of Ammonia from Dinitrogen on Iron Sulfide Surfaces

Dörr, M., Käßbohrer, J., Grunert, R., Kreisel, G., Brand, W. A., Werner, R. A., Geilmann, H., Apfel, C., Robl, C., & Weigand, W. (2003) · Angewandte Chemie International Edition · doi:10.1002/anie.200250371 · Cited by 132 · see citing works

Coenzyme A Biosynthesis: Reconstruction of the Pathway in Archaea and an Evolutionary Scenario Based on Comparative Genomics

Genschel, U. (2004) · Molecular Biology and Evolution · doi:10.1093/molbev/msh119 · Cited by 131 · see citing works

Elucidation of the biosynthesis of the methane catalyst coenzyme F430

Moore, S. J., Sowa, S. T., Schuchardt, C., Deery, E. C., Lawrence, A. D., Ramos, J. V., Billig, S., Birkemeyer, C., Chivers, P. T., Howard, M. J., et al. (2017) · Nature · doi:10.1038/nature21427 · Cited by 130 · see citing works

Vanadium nitrogenase: A two-hit wonder?

Hu, Y., Lee, C. C., & Ribbe, M. W. (2011) · Dalton Transactions · doi:10.1039/c1dt11535a · Cited by 129 · see citing works

Vitamins

Friedrich, W. (1988) · De Gruyter eBooks · doi:10.1515/9783110859188 · Cited by 129 · see citing works

Demonstration That the Radical S-Adenosylmethionine (SAM) Enzyme PqqE Catalyzes de Novo Carbon-Carbon Cross-linking within a Peptide Substrate PqqA in the Presence of the Peptide Chaperone PqqD

Barr, I., Latham, J. A., Iavarone, A. T., Chantarojsiri, T., Hwang, J. D., & Klinman, J. P. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.c115.699918 · Cited by 129 · see citing works

Elucidation of methanogenic coenzyme biosyntheses: from spectroscopy to genomics

Graham, D. E., & White, R. H. (2001) · Natural Product Reports · doi:10.1039/b103714p · Cited by 127 · see citing works

The origin and evolution of modern metabolism

Caetano‐Anollés, G., Yafremava, L. S., Gee, H., Caetano-Anollés, D., Kim, H. S., & Mittenthal, J. E. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.08.022 · Cited by 124 · see citing works

Atlas of the Radical SAM Superfamily: Divergent Evolution of Function Using a “Plug and Play” Domain

Holliday, G. L., Akiva, E., Meng, E. C., Brown, S. D., Calhoun, S., Pieper, U., Šali, A., Booker, S. J., & Babbitt, P. C. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.06.004 · Cited by 124 · see citing works

A theory of biochemical organization, metabolic pathways, and evolution

Morowitz, H. J. (1999) · Complexity · doi:10.1002/(sici)1099-0526(199907/08)4:6 · Cited by 122 · see citing works

The HydG Enzyme Generates an Fe(CO) 2 (CN) Synthon in Assembly of the FeFe Hydrogenase H-Cluster

Kuchenreuther, J. M., Myers, W. K., Suess, D. L. M., Stich, T. A., Pelmenschikov, V., Shiigi, S. A., Cramer, S. P., Swartz, J. R., Britt, R. D., & George, S. J. (2014) · Science · doi:10.1126/science.1246572 · Cited by 119 · see citing works

An appeal to magic? The discovery of a non-enzymatic metabolism and its role in the origins of life

Ralser, M. (2018) · Biochemical Journal · doi:10.1042/bcj20160866 · Cited by 117 · see citing works

A plausible metal-free ancestral analogue of the Krebs cycle composed entirely of α-ketoacids

Stubbs, R. T., Yadav, M., Krishnamurthy, R., & Springsteen, G. (2020) · Nature Chemistry · doi:10.1038/s41557-020-00560-7 · Cited by 117 · see citing works

Anaerobic biosynthesis of the lower ligand of vitamin B ₁₂

Hazra, A. B., Han, A. W., Mehta, A. P., Mok, K. C., Osadchiy, V., Begley, T. P., & Taga, M. E. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1509132112 · Cited by 116 · see citing works

On a Hypothetical Generational Relationship between HCN and Constituents of the Reductive Citric Acid Cycle

Eschenmoser, A. (2007) · Chemistry & Biodiversity · doi:10.1002/cbdv.200790050 · Cited by 115 · see citing works

Photolyase: Dynamics and electron-transfer mechanisms of DNA repair

Zhang, M., Wang, L., & Zhong, D. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.08.007 · Cited by 115 · see citing works

Thiamin diphosphate-dependent enzymes: from enzymology to metabolic regulation, drug design and disease models

Bunik, V. I., Tylicki, A., & Lukashev, N. V. (2013) · FEBS Journal · doi:10.1111/febs.12512 · Cited by 115 · see citing works

Elucidating biosynthetic pathways for vitamins and cofactors

Webb, M. E., Marquet, A., Mendel, R. R., Rébeillé, F., & Smith, A. G. (2007) · Natural Product Reports · doi:10.1039/b703105j · Cited by 113 · see citing works

Elucidation of the anaerobic pathway for the corrin component of cobalamin (vitamin B 12 )

Moore, S. J., Lawrence, A. D., Biedendieck, R., Deery, E. C., Frank, S., Howard, M. J., Rigby, S. E. J., & Warren, M. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1308098110 · Cited by 113 · see citing works

Pyridoxal phosphate: Biosynthesis and catabolism

Mukherjee, T., Hanes, J. W., Tews, I., Ealick, S. E., & Begley, T. P. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.06.018 · Cited by 111 · see citing works

A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation

Allen, J. R., Clark, D. D., Krum, J. G., & Ensign, S. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.15.8432 · Cited by 110 · see citing works

Functional diversity of organic molecule enzyme cofactors

Richter, M. (2013) · Natural Product Reports · doi:10.1039/c3np70045c · Cited by 109 · see citing works

Metals likely promoted protometabolism in early ocean alkaline hydrothermal systems

Kitadai, N., Nakamura, R., Yamamoto, M., Takai, K., Yoshida, N., & Oono, Y. (2019) · Science Advances · doi:10.1126/sciadv.aav7848 · Cited by 109 · see citing works

Mechanism of N2 Reduction Catalyzed by Fe-Nitrogenase Involves Reductive Elimination of H2

Harris, D. F., Lukoyanov, D. A., Shaw, S., Compton, P. D., Tokmina‐Lukaszewska, M., Bothner, B. B., Kelleher, N. L., Dean, D. R., Hoffman, B. M., & Seefeldt, L. C. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b01142 · Cited by 109 · see citing works

NAD ⁺ Biosynthesis and Signaling in Plants

Gakière, B., Hao, J., de Bont, L., Pétriacq, P., Nunes-Nesi, A., & Fernie, A. R. (2018) · Critical Reviews in Plant Sciences · doi:10.1080/07352689.2018.1505591 · Cited by 108 · see citing works

Coenzymes and their role in the evolution of life

Kirschning, A. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.201914786 · Cited by 107 · see citing works

The pyrroloquinoline quinone biosynthesis pathway revisited: A structural approach

Puehringer, S., Metlitzky, M., & Schwarzenbacher, R. (2008) · BMC Biochemistry · doi:10.1186/1471-2091-9-8 · Cited by 106 · see citing works

Structural Studies on 3-Hydroxyanthranilate-3,4-dioxygenase: The Catalytic Mechanism of a Complex Oxidation Involved in NAD Biosynthesis,

Zhang, Y., Colabroy, K. L., Begley, T. P., & Ealick, S. E. (2005) · Biochemistry · doi:10.1021/bi047353l · Cited by 106 · see citing works

Mechanistic and Mutational Studies of Escherichia coli Molybdopterin Synthase Clarify the Final Step of Molybdopterin Biosynthesis

Wuebbens, M. M., & Rajagopalan, K. V. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300453200 · Cited by 103 · see citing works

Deuterium Studies Reveal a New Mechanism for the Formose Reaction Involving Hydride Shifts

Appayee, C., & Breslow, R. (2014) · Journal of the American Chemical Society · doi:10.1021/ja410886c · Cited by 99 · see citing works

C–C bond forming radical SAM enzymes involved in the construction of carbon skeletons of cofactors and natural products

Yokoyama, K., & Lilla, E. A. (2018) · Natural Product Reports · doi:10.1039/c8np00006a · Cited by 99 · see citing works

Thiocarboxylation of Molybdopterin Synthase Provides Evidence for the Mechanism of Dithiolene Formation in Metal-binding Pterins

Gutzke, G., Fischer, B., Mendel, R. R., & Schwarz, G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105321200 · Cited by 95 · see citing works

Novel metabolic pathways in Archaea

Sato, T., & Atomi, H. (2011) · Current Opinion in Microbiology · doi:10.1016/j.mib.2011.04.014 · Cited by 93 · see citing works

The biosynthesis of porphyrins, chlorophylls, and vitamin B12

Leeper, F. J. (1989) · Natural Product Reports · doi:10.1039/np9890600171 · Cited by 93 · see citing works

Biosynthesis of Menaquinone (Vitamin K 2 ) and Ubiquinone (Coenzyme Q)

Meganathan, R., & Kwon, O. (2009) · EcoSal Plus · doi:10.1128/ecosalplus.3.6.3.3 · Cited by 90 · see citing works

Biosynthesis of ribose‐5‐phosphate and erythrose‐4‐phosphate in archaea: a phylogenetic analysis of archaeal genomes

Soderberg, T. (2004) · Archaea · doi:10.1155/2005/314760 · Cited by 85 · see citing works

A Cytosine Methyltransferase Converts 5-Methylcytosine in DNA to Thymine

Yebra, M. J., & Bhagwat, A. S. (1995) · Biochemistry · doi:10.1021/bi00045a016 · Cited by 83 · see citing works

Advances in bacterial pathways for the biosynthesis of ubiquinone

Abby, S. S., Kazemzadeh, K., Vragniau, C., Pélosi, L., & Pierrel, F. (2020) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2020.148259 · Cited by 83 · see citing works

The Futalosine Pathway Played an Important Role in Menaquinone Biosynthesis during Early Prokaryote Evolution

Zhi, X., Yao, J.-C., Tang, S., Huang, Y., Li, H.-W., & Li, W. (2014) · Genome Biology and Evolution · doi:10.1093/gbe/evu007 · Cited by 82 · see citing works

l -Aspartate Semialdehyde and a 6-Deoxy-5-ketohexose 1-Phosphate Are the Precursors to the Aromatic Amino Acids in Methanocaldococcus jannaschii

White, R. H. (2004) · Biochemistry · doi:10.1021/bi0495127 · Cited by 80 · see citing works

Quinolinate synthetase, an iron–sulfur enzyme in NAD biosynthesis

de Choudens, S. O., Loiseau, L., Sanakis, Y., Barras, F., & Fontecave, M. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.05.065 · Cited by 80 · see citing works

Rotary DNA motors

Doering, C. R., Ermentrout, B., & OSTER, G. F. (1995) · Biophysical Journal · doi:10.1016/s0006-3495(95)80096-2 · Cited by 77 · see citing works

The Structures and Physicochemical Properties of Organic Cofactors in Biocatalysis

Fischer, J. D., Holliday, G. L., Rahman, S. A., & Thornton, J. M. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.09.018 · Cited by 76 · see citing works

An Interpretive Review of the Origin of Life Research

Penny, D. (2005) · Biology & Philosophy · doi:10.1007/s10539-004-7342-6 · Cited by 76 · see citing works

Radical S-Adenosylmethionine (SAM) Enzymes in Cofactor Biosynthesis: A Treasure Trove of Complex Organic Radical Rearrangement Reactions

Mehta, A. P., Abdelwahed, S. H., Mahanta, N., Fedoseyenko, D., Philmus, B. J., Cooper, L. E., Liu, Y., Jhulki, I., Ealick, S. E., & Begley, T. P. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.623793 · Cited by 76 · see citing works

Biosynthesis of nitrogenase FeMoco

Hu, Y., & Ribbe, M. W. (2010) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2010.11.018 · Cited by 74 · see citing works

Catalytic Activity of the Anaerobic Tyrosine Lyase Required for Thiamine Biosynthesis in Escherichia coli

Challand, M. R., Martins, F., & Roach, P. L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.056606 · Cited by 71 · see citing works

Biosynthesis of F 0 , Precursor of the F 420 Cofactor, Requires a Unique Two Radical-SAM Domain Enzyme and Tyrosine as Substrate

Decamps, L., Philmus, B. J., Benjdia, A., White, R. H., Begley, T. P., & Berteau, O. (2012) · Journal of the American Chemical Society · doi:10.1021/ja307762b · Cited by 71 · see citing works

A general model on the origin of biological codes

Barbieri, M. (2019) · Biosystems · doi:10.1016/j.biosystems.2019.04.010 · Cited by 70 · see citing works

Reconstruction of the Central Carbohydrate Metabolism of Thermoproteus tenax by Use of Genomic and Biochemical Data

Siebers, B., Tjaden, B., Michalke, K., Dörr, C., Ahmed, H., Zaparty, M., Gordon, P. M. K., Sensen, C. W., Zibat, A., Klenk, H., et al. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.7.2179-2194.2004 · Cited by 70 · see citing works

Evolution of folate biosynthesis and metabolism across algae and land plant lineages

Gorelova, V., Bastien, O., Clerck, O. D., Lespinats, S., Rébeillé, F., & Straeten, D. V. D. (2019) · Scientific Reports · doi:10.1038/s41598-019-42146-5 · Cited by 69 · see citing works

Biosynthesis and Activity of Prenylated FMN Cofactors

Wang, P., Khusnutdinova, A. N., Luo, F., Xiao, J. Z., Nemr, K., Flick, R., Brown, G., Mahadevan, R., Edwards, E. A., & Yakunin, A. F. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.02.007 · Cited by 69 · see citing works

Evolution of enzymes and pathways for the biosynthesis of cofactors

Holliday, G. L., Thornton, J. M., Marquet, A., Smith, A. G., Rébeillé, F., Mendel, R., Schubert, H. L., Lawrence, A. D., & Warren, M. J. (2007) · Natural Product Reports · doi:10.1039/b703107f · Cited by 68 · see citing works

Prebiotic Chemistry that Could Not Not Have Happened

Benner, S. A., Kim, H.-J., & Biondi, E. (2019) · Life · doi:10.3390/life9040084 · Cited by 66 · see citing works

Cofactor biosynthesis: an organic chemist's treasure trove

Begley, T. P. (2006) · Natural Product Reports · doi:10.1039/b207131m · Cited by 63 · see citing works

Giving Rise to Life: Transition from Prebiotic Chemistry to Protobiology

Krishnamurthy, R. (2017) · Accounts of Chemical Research · doi:10.1021/acs.accounts.6b00470 · Cited by 63 · see citing works

Life as a guide to prebiotic nucleotide synthesis

Harrison, S. A., & Lane, N. (2018) · Nature Communications · doi:10.1038/s41467-018-07220-y · Cited by 63 · see citing works

Prebiotic synthesis of histidine

Shen, C., Yang, L., Miller, S. L., & Oro, J. A. (1990) · Journal of Molecular Evolution · doi:10.1007/bf02109492 · Cited by 61 · see citing works

NAD Biosynthesis Evolution in Bacteria: Lateral Gene Transfer of Kynurenine Pathway in Xanthomonadales and Flavobacteriales

de Lima, W. C., Varani, A. M., & Menck, C. F. M. (2008) · Molecular Biology and Evolution · doi:10.1093/molbev/msn261 · Cited by 61 · see citing works

Mechanism of pyranopterin ring formation in molybdenum cofactor biosynthesis

Hover, B. M., Tonthat, N. K., Schumacher, M. A., & Yokoyama, K. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1500697112 · Cited by 60 · see citing works

Did primitive microorganisms use nonhem iron proteins in place of NAD/P?

Daniel, R. M., & Danson, M. J. (1995) · Journal of Molecular Evolution · doi:10.1007/bf00160501 · Cited by 59 · see citing works

The Structure of a Biosynthetic Intermediate of Pyrroloquinoline Quinone (PQQ) and Elucidation of the Final Step of PQQ Biosynthesis

Magnússon, Ó. Þ., Toyama, H., Saeki, M., Schwarzenbacher, R., & Klinman, J. P. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0493852 · Cited by 59 · see citing works

Nicotinic Acid Biosynthesis in Prototrophs and Tryptophan Auxotrophs of Saccharomyces cerevisiae

Ahmad, F., & Moat, A. G. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96832-8 · Cited by 59 · see citing works

Radical SAM Enzyme HydE Generates Adenosylated Fe(I) Intermediates En Route to the [FeFe]-Hydrogenase Catalytic H‑Cluster

Tao, L., Pattenaude, S. A., Joshi, S., Begley, T. P., Rauchfuss, T. B., & Britt, R. D. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c03802 · Cited by 59 · see citing works

Chemical Diversity of Metal Sulfide Minerals and Its Implications for the Origin of Life

Li, Y., Kitadai, N., & Nakamura, R. (2018) · Life · doi:10.3390/life8040046 · Cited by 58 · see citing works

Structure and chemistry of 4-methylideneimidazole-5-one containing enzymes

Cooke, H. A., Christianson, C. V., & Bruner, S. D. (2009) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2009.06.013 · Cited by 57 · see citing works

On the Origin of Iron/Sulfur Cluster Biosynthesis in Eukaryotes

Tsaousis, A. D. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.02478 · Cited by 56 · see citing works

Unraveling the Pathway of Lipoic Acid Biosynthesis

Booker, S. J. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.01.002 · Cited by 55 · see citing works

Abundance of 4Fe–4S motifs in the genomes of methanogens and other prokaryotes

Major, T. A., Burd, H., & Whitman, W. B. (2004) · FEMS Microbiology Letters · doi:10.1016/j.femsle.2004.08.027 · Cited by 55 · see citing works

Riboflavin analogs and inhibitors of riboflavin biosynthesis

Mack, M., & Grill, S. (2006) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-006-0421-7 · Cited by 54 · see citing works

A “Radical Dance” in Thiamin Biosynthesis: Mechanistic Analysis of the Bacterial Hydroxymethylpyrimidine Phosphate Synthase

Chatterjee, A., Hazra, A. B., Abdelwahed, S. H., Hilmey, D. G., & Begley, T. P. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201003419 · Cited by 53 · see citing works

Metal Catalysts and the Origin of Life

Belmonte, L., & Mansy, S. S. (2016) · Elements · doi:10.2113/gselements.12.6.413 · Cited by 53 · see citing works

Evolution of the genetic code: The ambiguity-reduction theory

Barbieri, M. (2019) · Biosystems · doi:10.1016/j.biosystems.2019.104024 · Cited by 53 · see citing works

The Thiamine Biosynthetic Enzyme ThiC Catalyzes Multiple Turnovers and Is Inhibited by S-Adenosylmethionine (AdoMet) Metabolites

Palmer, L. D., & Downs, D. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.500280 · Cited by 53 · see citing works

CO and CN − syntheses by [FeFe]-hydrogenase maturase HydG are catalytically differentiated events

Pagnier, A., Martin, L., Zeppieri, L., Nicolet, Y., & Fontecilla-Camps, J. C. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1515842113 · Cited by 53 · see citing works

A [4Fe–4S]-Fe(CO)(CN)-l-cysteine intermediate is the first organometallic precursor in [FeFe] hydrogenase H-cluster bioassembly

Rao, G., Tao, L., Suess, D. L. M., & Britt, R. D. (2018) · Nature Chemistry · doi:10.1038/s41557-018-0026-7 · Cited by 53 · see citing works

The Nicotinamide Biosynthetic Pathway Is a By-Product of the RNA World

Cleaves, H. J., & Miller, S. L. (2001) · Journal of Molecular Evolution · doi:10.1007/s002390010135 · Cited by 52 · see citing works

A Survey of Pyridoxal 5′-Phosphate-Dependent Proteins in the Gram-Positive Model Bacterium Bacillus subtilis

Richts, B., Rosenberg, J., & Commichau, F. M. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00032 · Cited by 52 · see citing works

Phenylalanine and Tyrosine Synthesis under Primitive Earth Conditions

Friedmann, N., & Miller, S. L. (1969) · Science · doi:10.1126/science.166.3906.766 · Cited by 51 · see citing works

Molecular Insights into the Biosynthesis of the F420 Coenzyme

Forouhar, F., Abashidze, M., Xu, H., Grochowski, L. L., Seetharaman, J., Hussain, M., Kuzin, A. P., Yang, C., Zhou, W., Xiao, R., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710352200 · Cited by 51 · see citing works

Thiamin Pyrimidine Biosynthesis in Candida albicans: A Remarkable Reaction between Histidine and Pyridoxal Phosphate

Lai, R., Huang, S., Fenwick, M. K., Hazra, A. B., Zhang, Y., Rajashankar, K. R., Philmus, B. J., Kinsland, C. L., Sanders, J. M., Ealick, S. E., et al. (2012) · Journal of the American Chemical Society · doi:10.1021/ja302474a · Cited by 50 · see citing works

5′-Methylthioadenosine Nucleosidase Is Implicated in Playing a Key Role in a Modified Futalosine Pathway for Menaquinone Biosynthesis in Campylobacter jejuni

Li, X., Apel, D., Gaynor, E. C., & Tanner, M. E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.229781 · Cited by 47 · see citing works

Cofactor biosynthesis—still yielding fascinating new biological chemistry

Begley, T. P., Chatterjee, A., Hanes, J. W., Hazra, A. B., & Ealick, S. E. (2008) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2008.02.006 · Cited by 46 · see citing works

Emerging themes in radical SAM chemistry

Shisler, K. A., & Broderick, J. B. (2012) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2012.10.005 · Cited by 46 · see citing works

Biochemical Constraints in a Protobiotic Earth Devoid of Basic Amino Acids: The “BAA(-) World”

McDonald, G. D., & Storrie‐Lombardi, M. C. (2010) · Astrobiology · doi:10.1089/ast.2010.0484 · Cited by 43 · see citing works

Metal and cofactor insertion

Mendel, R. R., Smith, A. G., Marquet, A., & Warren, M. J. (2007) · Natural Product Reports · doi:10.1039/b703112m · Cited by 43 · see citing works

On the Evolutionary History of the Twenty Encoded Amino Acids

Kirschning, A. (2022) · Chemistry - A European Journal · doi:10.1002/chem.202201419 · Cited by 43 · see citing works

Novel enzymology in futalosine-dependent menaquinone biosynthesis

Joshi, S., Fedoseyenko, D., Mahanta, N., Manion, H. R., Naseem, S., Dairi, T., & Begley, T. P. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2018.09.015 · Cited by 43 · see citing works

Flavin metamorphosis: cofactor transformation through prenylation

Leys, D. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2018.09.024 · Cited by 42 · see citing works

Recreating ancient metabolic pathways before enzymes

Muchowska, K. B., Chevallot-Béroux, E., & Moran, J. (2019) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2019.03.012 · Cited by 42 · see citing works

Methylglyoxal Is an Intermediate in the Biosynthesis of 6-Deoxy-5-ketofructose-1-phosphate: A Precursor for Aromatic Amino Acid Biosynthesis in Methanocaldococcus jannaschii

White, R. H., & Xu, H. (2006) · Biochemistry · doi:10.1021/bi061018a · Cited by 41 · see citing works

Iron–sulfur proteins as initiators of radical chemistry

Marquet, A., Bui, B. T. S., Smith, A. G., & Warren, M. J. (2007) · Natural Product Reports · doi:10.1039/b703109m · Cited by 41 · see citing works

From Suicide Enzyme to Catalyst: The Iron-Dependent Sulfide Transfer in Methanococcus jannaschii Thiamin Thiazole Biosynthesis

Eser, B. E., Zhang, X. K., Chanani, P. K., Begley, T. P., & Ealick, S. E. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b00445 · Cited by 41 · see citing works

A Direct Prebiotic Synthesis of Nicotinamide Nucleotide

Kim, H., & Benner, S. A. (2017) · Chemistry - A European Journal · doi:10.1002/chem.201705394 · Cited by 40 · see citing works

Evolution of Vitamin B2 Biosynthesis. A Novel Class of Riboflavin Synthase in Archaea

Fischer, M. J., Schott, A.-K., Römisch, W., Ramsperger, A., Augustin, M. A., Fidler, A., Bacher, A., Richter, G., Huber, R., & Eisenreich, W. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.08.016 · Cited by 40 · see citing works

Studies on the biosynthesis of coenzyme F420 in methanogenic bacteria

Jaenchen, R., Sch�nheit, P., & Thauer, R. K. (1984) · Archives of Microbiology · doi:10.1007/bf00410735 · Cited by 39 · see citing works

H-Cluster assembly during maturation of the [FeFe]-hydrogenase

Broderick, J. B., Byer, A. S., Duschene, K. S., Duffus, B. R., Betz, J. N., Shepard, E. M., & Peters, J. W. (2014) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-014-1168-8 · Cited by 38 · see citing works

Evidence from glycine transfer RNA of a frozen accident at the dawn of the genetic code

Bernhardt, H. S., & Tate, W. P. (2008) · Biology Direct · doi:10.1186/1745-6150-3-53 · Cited by 36 · see citing works

Identification of Enzymes Homologous to Isocitrate Dehydrogenase That Are Involved in Coenzyme B and Leucine Biosynthesis in Methanoarchaea

Howell, D. M., Graupner, M., Xu, H., & White, R. H. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.17.5013-5016.2000 · Cited by 35 · see citing works

Biosynthetic precursors of deazaflavins

Reuke, B., Korn, S., Eisenreich, W., & Bacher, A. (1992) · Journal of Bacteriology · doi:10.1128/jb.174.12.4042-4049.1992 · Cited by 34 · see citing works

Genetic Code Evolution Started with the Incorporation of Glycine, Followed by Other Small Hydrophilic Amino Acids

Bernhardt, H. S., & Patrick, W. M. (2014) · Journal of Molecular Evolution · doi:10.1007/s00239-014-9627-y · Cited by 33 · see citing works

L-Aspartate oxidase is present in the anaerobic hyperthermophilic archaeon Pyrococcus horikoshii OT-3: characteristics and role in the de novo biosynthesis of nicotinamide adenine dinucleotide proposed by genome sequencing

Sakuraba, H., Satomura, T., Kawakami, R., Yamamoto, S., Kawarabayasi, Y., Kikuchi, H., & Ohshima, T. (2002) · Extremophiles · doi:10.1007/s00792-001-0254-3 · Cited by 33 · see citing works

Activation of the Anaerobic Ribonucleotide Reductase by S ‐Adenosylmethionine

Gambarelli, S., Luttringer, F., Padovani, D., Mulliez, E., & Fontecave, M. (2005) · ChemBioChem · doi:10.1002/cbic.200500182 · Cited by 31 · see citing works

Prebiotic synthesis of imidazole-4-acetaldehyde and histidine

Shen, C., Yang, L. P. H., Miller, S. L., & Oro, J. A. (1987) · Origins of Life and Evolution of Biospheres · doi:10.1007/bf02386469 · Cited by 31 · see citing works

Structure of 3,4-Dihydroxy-2-butanone 4-Phosphate Synthase from Methanococcus jannaschii in Complex with Divalent Metal Ions and the Substrate Ribulose 5-Phosphate

Steinbacher, S., Schiffmann, S., Richter, G., Huber, R., Bacher, A., & Fischer, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307301200 · Cited by 30 · see citing works

Biosynthesis of Riboflavin in Archaea Studies on the Mechanism of 3,4-Dihydroxy-2-butanone-4-phosphate Synthase of Methanococcus jannaschii

Fischer, M. J., Römisch, W., Schiffmann, S., Kelly, M. J. S., Oschkinat, H., Steinbacher, S., Huber, R., Eisenreich, W., Richter, G., & Bacher, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206863200 · Cited by 30 · see citing works

Iron: Life’s primeval transition metal

Johnson, J. E., Present, T. M., & Valentine, J. S. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2318692121 · Cited by 48 · see citing works

Revitalising Riboflavin: Unveiling Its Timeless Significance in Human Physiology and Health

Aragão, M. Â., Pires, L., Santos‐Buelga, C., Barros, L., & Calhelha, R. C. (2024) · Foods · doi:10.3390/foods13142255 · Cited by 48 · see citing works

Metal ions turn on a stereoselective nonenzymatic reduction of keto acids by the coenzyme NADH

Mayer, R. J., & Moran, J. (2024) · Chem · doi:10.1016/j.chempr.2024.05.007 · Cited by 29 · see citing works

Pinpointing Conditions for a Metabolic Origin of Life: Underlying Mechanisms and the Role of Coenzymes

Zimmermann, J., Werner, E., Sodei, S., & Moran, J. (2024) · Accounts of Chemical Research · doi:10.1021/acs.accounts.4c00423 · Cited by 25 · see citing works

Phages in vermicomposts enrich functional gene content and facilitate pesticide degradation in soil

Chao, H., Balcázar, J. L., Wu, Y., Cai, A., Ye, M., Sun, M., & Hu, F. (2023) · Environment International · doi:10.1016/j.envint.2023.108175 · Cited by 22 · see citing works

A path to perpetual chemical synthesis via photocatalytic cofactor regeneration

Jain, V., & Pillai, P. P. (2025) · Chemical Science · doi:10.1039/d5sc02770e · Cited by 20 · see citing works

Evidence for corrin biosynthesis in the last universal common ancestor

Modjewski, L. D., Karavaeva, V., Mrnjavac, N., Knopp, M., Martin, W. F., & Sousa, F. L. (2025) · The FEBS Journal · doi:10.1111/febs.17367 · Cited by 15 · see citing works

The Role of Sulfhydryl (Thiols) Groups in Oral and Periodontal Diseases

ÇERKEZI, S., Nakova, M., Gorgoski, I., Ferati, K., Bexheti‐Ferati, A., Palermo, A., Inchingolo, A. D., Ferrante, L., Inchingolo, A. M., Inchingolo, F., et al. (2024) · Biomedicines · doi:10.3390/biomedicines12040882 · Cited by 15 · see citing works

Evolution at the Origins of Life?

Schoenmakers, L. L. J., Reydon, T. A. C., & Kirschning, A. (2024) · Life · doi:10.3390/life14020175 · Cited by 14 · see citing works

A Prebiotic Pathway to Nicotinamide Adenine Dinucleotide

Bechtel, M. A., Kurrle, N. J., & Trapp, O. (2024) · Chemistry - A European Journal · doi:10.1002/chem.202402055 · Cited by 13 · see citing works

Reagent Engineering for Group Transfer Biocatalysis

Reed, J. H., & Seebeck, F. P. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202311159 · Cited by 11 · see citing works

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Kazemzadeh, K., Pélosi, L., Chenal, C., Chobert, S.-C., Chehade, M. H., Jullien, M., Flandrin, L., Schmitt, W., He, Q., Bouvet, E., et al. (2023) · Molecular Biology and Evolution · doi:10.1093/molbev/msad219 · Cited by 11 · see citing works

Translation Fidelity and Respiration Deficits in CLPP-Deficient Tissues: Mechanistic Insights from Mitochondrial Complexome Profiling

Key, J., Gispert, S., Koepf, G., Steinhoff‐Wagner, J., Reichlmeir, M., & Auburger, G. W. J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417503 · Cited by 8 · see citing works

Convergent Evolution of Coenzyme Metabolism in Methanosarcina mazei: Insights Into Primitive Life and Metabolic Adaptations

Saranya, S., & Chellapandi, P. (2025) · Journal of Basic Microbiology · doi:10.1002/jobm.70015 · Cited by 7 · see citing works

Intermediate stages in the origin of metabolism at a phosphorylating hydrothermal vent

Mrnjavac, N., Hoffmann, N. K., Schlikker, M. L., Burmeister, M., Schwander, L., Garcia, C. G., Brabender, M., Steel, M., Huson, D., Metzger, S., et al. (2025) · Science Advances · doi:10.1126/sciadv.aef3128 · Cited by 4 · see citing works

Why pyridoxal phosphate could be a functional predecessor of thiamine pyrophosphate and speculations on a primordial metabolism

Kirschning, A. (2024) · RSC Chemical Biology · doi:10.1039/d4cb00016a · Cited by 5 · see citing works

Swine-Derived Probiotics and Their Metabolites as an Alternative to Veterinary Antibiotics

Zhao, M., Chen, B., Song, P. Y., Mei, G. D., Li, M., Lin, F., Sun, T., & Li, Z. (2025) · Veterinary Sciences · doi:10.3390/vetsci12111100 · Cited by 5 · see citing works

Chemistry of Coenzyme F420 in Environment

Chauhan, S. M. S. (2024) · Journal of Molecular Chemistry. · doi:10.62110/sciencein.jmc.2024.696 · Cited by 5 · see citing works

Nickel: Geochemistry, biochemistry and its role in chemical and biological evolutions

Neubeck, A., & Kirschning, A. (2025) · Earth-Science Reviews · doi:10.1016/j.earscirev.2025.105324 · Cited by 4 · see citing works

Structural and functional consequences of aspartate/asparagine-β-hydroxylase variants causing Traboulsi syndrome

Hou, C., Brasnett, A., Rabe, P., Schofield, C. J., & Brewitz, L. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.111008 · Cited by 3 · see citing works

S -Adenosylmethionine: considerations on its role in the origin and evolution of life

Kirschning, A. (2026) · Natural Product Reports · doi:10.1039/d5np00079c · Cited by 4 · see citing works

Structure and Substrate Specificity of S-Methyl Thiourocanate Hydratase

Vasseur, C. M., Karunasegaram, D., & Seebeck, F. P. (2024) · ACS Chemical Biology · doi:10.1021/acschembio.3c00745 · Cited by 3 · see citing works

Fungal Metabolites as Natural Flavor Enhancers

Vasisht, R., Yadav, J., & Agnihotri, S. (2025) · Fungal biology · doi:10.1007/978-3-032-04519-5_7 · Cited by 2 · see citing works

Terpene synthases are highly substrate tolerant – among them BcBOT2 is a “jack of all trades”

Budde, J. L., Davari, M. D., Hassanin, A., Karacam, M., Kirschning, A., Struwe, H., & Taser, D. (2026) · Natural Product Reports · doi:10.1039/d6np00040a · Cited by 2 · see citing works

Transcriptome and proteome changes triggered by overexpression of the transcriptional regulator Maf1 in the human pathogen Leishmania major

Rivera-Rivas, L. A., Florencio-Martínez, L. E., Romero‐Meza, G., Ortega‐Ortiz, R. C., Manning-Cela, R. G., Carrero, J. C., Nepomuceno‐Mejía, T., & Martínez‐Calvillo, S. (2024) · The FASEB Journal · doi:10.1096/fj.202400636rr · Cited by 2 · see citing works

Reagent Engineering for Group Transfer Biocatalysis

Reed, J. H., & Seebeck, F. P. (2023) · Angewandte Chemie · doi:10.1002/ange.202311159 · Cited by 1 · see citing works

Organic Cofactors in the Electron Transport Chain: Properties and Connection to the Prebiotic World

Riazi‐Sekowski, S., Bundang, K., Chastain, J. L., Carman, N., Velling, S. J., Aguilera, J., Luna, M., Trejo, C., Alian, O. M., Teece, B. L., et al. (2026) · ChemSystemsChem · doi:10.1002/syst.202500037 · Cited by 1 · see citing works

A Nonenzymatic Analogue of the Biosynthesis of Pyridoxal Vitamers

Nogal, N., Basar, A. B., Minić, Z., & Moran, J. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c01677 · Cited by 1 · see citing works

Synthesis, Photophysical Properties, and Molecular Docking Studies of New Nitropyridine Linked 4-Arylidene-thiazolidin-4-ones (D-π-A Structured) as Potent Anticancer Agents

Jame, R. (2024) · Russian Journal of Organic Chemistry · doi:10.1134/s1070428024070236 · Cited by 1 · see citing works

The dinucleotide structure of NAD enables specific reduction on mineral surfacesPreprint

Pereira, D. P. H., Xie, X., Beyazay, T., Paczia, N., Subrati, Z., Belz, J., Volz, K., Tüysüz, H., & Preiner, M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.11.617347

Koenzyme als Verbindungsstücke zwischen Geo- und Biochemie

Pereira, D. P. H., & Preiner, M. (2025) · BIOspektrum · doi:10.1007/s12268-025-2569-7

Discovering new anti-methanogenic compounds to reduce enteric methane emissions from rumen methanogensPreprint

Chai, H.-H., Park, W., Wi, J., Jin, Y. B., & Lim, D. (2026) · SSRN Electronic Journal · doi:10.2139/ssrn.6041977

NAD+ Homeostasis and Mitochondrial Modifiability: Resilience in Alzheimer’s Disease

Stefano, G. B. (2026) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl49714

Etudes des voies de biosynthèse de l’ubiquinone chez les protéobactéries

Kazemzadeh, K. (2023) · theses.fr (ABES) · doi:10.70675/a6cc3367z0383z404az87fczc09a7490e517

Präbiotische Chemie – vom Stoffwechsel aus gedacht/Trendbericht Biochemie 2026 3/4

Preiner, M. (2026) · Nachrichten aus der Chemie · doi:10.1002/nadc.20264156443

Pyrroloquinoline quinone protects heat-stressed porcine oocytes and improves early embryonic development via maintaining mitochondrial integrity and redox homeostasis

Zhang, M., Xu, Q., Jia, B., Zhang, X., Lay, K., Li, M., Zou, Y., Wang, Z., Peng, X., Gao, Y., et al. (2026) · Biology Direct · doi:10.1186/s13062-026-00845-w

From o ‐Phenylenediamine to Flavin Derivatives: A Potential Prebiotic Carbon Skeleton Expansion With Formaldehyde, Cyanide, and CO 2

Held, C., Lima, R. J. D. S., & Lee, J. (2026) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.70675

Evolution of the coenzymes

King, G. A. (1980) · Biosystems · doi:10.1016/0303-2647(80)90003-9 · Cited by 52 · see citing works

Evolution of enzymes and pathways for the biosynthesis of cofactors

Holliday, G. L., Thornton, J. M., Marquet, A., Smith, A. G., Rébeillé, F., Mendel, R., Schubert, H. L., Lawrence, A. D., & Warren, M. J. (2007) · Natural Product Reports · doi:10.1039/b703107f · Cited by 68 · see citing works

[Symposium. Biosynthesis of coenzymes].

(1966) · PubMed

Cofactor Biosynthesis

Haase, I., Fischer, M. J., Bacher, A., Eisenreich, W., & Rohdich, F. (2008) · Wiley eBooks · doi:10.1002/9780470048672.wecb094

Coenzyme und ihre Rolle in der Evolution des Lebens

Kirschning, A. (2020) · Angewandte Chemie · doi:10.1002/ange.201914786 · Cited by 2 · see citing works