Cited by 268Sulfur Compounds in BiologyRedox biology and oxidative stressMicrobial metabolism and enzyme function

The DOI matches its Crossref record; 135 of the 135 references it cites were found in a registry or an index.

Novel Thiols of Prokaryotes

Fahey, Robert C.·2001·Annual Review of Microbiology

Open this paper in CoChat — free account

Abstract

▪ Abstract Glutathione metabolism is associated with oxygenic cyanobacteria and the oxygen-utilizing purple bacteria, but is absent in many other prokaryotes. This review focuses on novel thiols found in those bacteria lacking glutathione. Included are glutathione amide and its perthiol, produced by phototrophic purple sulfur bacteria and apparently involved in their sulfide metabolism. Among archaebacteria, coenzyme M (2-mercaptoethanesulfonic acid) and coenzyme B (7-mercaptoheptanoylthreonine phosphate) play central roles in the anaerobic production of CH 4 and associated energy conversion by methanogens, whereas the major thiol in the aerobic phototrophic halobacteria is γ-glutamylcysteine. The highly aerobic actinomycetes produce mycothiol, a conjugate of N-acetylcysteine with a pseudodisaccharide of glucosamine and myo-inositol, AcCys-GlcNα(1 → 1)Ins, which appears to play an antioxidant role similar to glutathione. Ergothioneine, also produced by actinomycetes, remains a mystery despite many years of study. Available data on the biosynthesis and metabolism of these and other novel thiols is summarized and key areas for additional study are identified.

Integrity signals

Registry

Crossref · 10.1146/annurev.micro.55.1.333

Cites

135 of 135 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
Cole, S. T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S. V., Eiglmeier, K., Gas, S., Barry, C. E., et al. (1998) · Nature · doi:10.1038/31159 · Cited by 7,847
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
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 1,142
METABOLISM AND FUNCTIONS OF TRYPANOTHIONE IN THE KINETOPLASTIDA
Fairlamb, A. H., & Cerami, A. (1992) · Annual Review of Microbiology · doi:10.1146/annurev.mi.46.100192.003403 · Cited by 769
Biochemistry of the SH group
Jocelyn, P. C. (1972) · Cited by 699
Trypanothione: A Novel Bis(glutathionyl)spermidine Cofactor for Glutathione Reductase in Trypanosomatids
Fairlamb, A. H., Blackburn, P., Ulrich, P. C., Chait, B. T., & Cerami, A. (1985) · Science · doi:10.1126/science.3883489 · Cited by 685
Intracellular Antioxidants: from Chemical to Biochemical Mechanisms
Chaudière, J., & Ferrari-Iliou, R. (1999) · Food and Chemical Toxicology · doi:10.1016/s0278-6915(99)00090-3 · Cited by 671
Peptides by Activation of Amino Acids with CO on (Ni,Fe)S Surfaces: Implications for the Origin of Life
Huber, C., & Wächtershäuser, G. (1998) · Science · doi:10.1126/science.281.5377.670 · Cited by 645
Crystal Structure of Methyl-Coenzyme M Reductase: The Key Enzyme of Biological Methane Formation
Ermler, U., Grabarse, W., Shima, S., Goubeaud, M., & Thauer, R. K. (1997) · Science · doi:10.1126/science.278.5342.1457 · Cited by 615
THE STRUCTURE AND BIOSYNTHESIS OF GLYCOSYL PHOSPHATIDYLINOSITOL PROTEIN ANCHORS
Englund, P. T. (1993) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.62.070193.001005 · Cited by 590

Show all 133 references

Research works printed but not linked: 7

Dolphin D, 1989, Glutathione: Chemical, Biochemical, and Medical Aspects, Parts A and B.
Fairlamb AH, 1999, Medicina, 59, 179
10.1016/S0168-6445(98)00035-7 · DOI
Melville DB, 1957, J. Bacteriol., 224, 871
Newton GL, Fahey RC. 1989. Glutathione in procaryotes. InGlutathione: Metabolism and Physiological Functions, ed. J Viña, pp. 69–77. Boca Raton, FL: CRC Press
Tabor H, 1976, Italian J. Biochem., 25, 70
Tanret MC, 1909, Compt. Rend., 49, 222

Sorted by citations

Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging
Jomova, K., Raptova, R., Alomar, S. Y., Alwasel, S. H., Nepovimova, E., Kuca, K., & Valko, M. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03562-9 · Cited by 2,638
The thioredoxin antioxidant system
Lu, J., & Holmgren, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.036 · Cited by 2,055
Efflux-mediated heavy metal resistance in prokaryotes
Nies, D. H. (2003) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(03)00048-2 · Cited by 1,567
Redox Regulation in Photosynthetic Organisms: Signaling, Acclimation, and Practical Implications
Foyer, C. H., & Noctor, G. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2177 · Cited by 1,468
Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes
Deponte, M. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.09.018 · Cited by 1,150
Photoageing: mechanism, prevention and therapy
Yaar, M., & Gilchrest, B. A. (2007) · British Journal of Dermatology · doi:10.1111/j.1365-2133.2007.08108.x · Cited by 755
Glutaredoxins: Glutathione-Dependent Redox Enzymes with Functions Far Beyond a Simple Thioredoxin Backup System
Fernandes, A. P., & Holmgren, A. (2004) · Antioxidants and Redox Signaling · doi:10.1089/152308604771978354 · Cited by 670
Coenzyme A: Back in action
LEONARDI, R., Zhang, Y., ROCK, C., & Jackowski, S. (2005) · Progress in Lipid Research · doi:10.1016/j.plipres.2005.04.001 · Cited by 649
Glutathione transferases: substrates, inihibitors and pro-drugs in cancer and neurodegenerative diseases
Allocati, N., Masulli, M., Di Ilio, C., & Federici, L. (2018) · Oncogenesis · doi:10.1038/s41389-017-0025-3 · Cited by 625
Phylogenomics and Comparative Genomic Studies Robustly Support Division of the Genus Mycobacterium into an Emended Genus Mycobacterium and Four Novel Genera
Gupta, R. S., Lo, B., & Son, J. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.00067 · Cited by 562
The Many Faces of Glutathione in Bacteria
Masip, L., Veeravalli, K., & Georgiou, G. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.753 · Cited by 478
Inositol derivatives: evolution and functions
Michell, R. H. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2334 · Cited by 427
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
Glutathione transferases in bacteria
Allocati, N., Federici, L., Masulli, M., & Ilio, C. D. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06743.x · Cited by 366
Confocal imaging of glutathione redox potential in living plant cells
Schwarzländer, M., Fricker, M. D., Müller, C., Marty, L., Brach, T., Novák, J., Sweetlove, L. J., Hell, R., & Meyer, A. J. (2008) · Journal of Microscopy · doi:10.1111/j.1365-2818.2008.02030.x · Cited by 345
Potential role of glutathione in evolution of thiol-based redox signaling sites in proteins
Mohanasundaram, K. A., Haworth, N. L., Grover, M. P., Crowley, T. M., Goscinski, A. M., & Wouters, M. A. (2015) · Frontiers in Pharmacology · doi:10.3389/fphar.2015.00001 · Cited by 326
Glutathione, Altruistic Metabolite in Fungi
Pócsi, I., Prade, R. A., & Penninckx, M. J. (2004) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/s0065-2911(04)49001-8 · Cited by 311
Emerging role of hydrogen sulfide in health and disease: critical appraisal of biomarkers and pharmacological tools
Whiteman, M., Trionnaire, S. L., Chopra, M., Fox, B. C., & Whatmore, J. L. (2011) · Clinical Science · doi:10.1042/cs20110267 · Cited by 310
In Vitro Reconstitution of Mycobacterial Ergothioneine Biosynthesis
Seebeck, F. P. (2010) · Journal of the American Chemical Society · doi:10.1021/ja101721e · Cited by 293
The biology of ergothioneine, an antioxidant nutraceutical
Borodina, I., Kenny, L. C., McCarthy, C. M., Paramasivan, K., Pretorius, E., Roberts, T. J., van der Hoek, S. A., & Kell, D. B. (2020) · Nutrition Research Reviews · doi:10.1017/s0954422419000301 · Cited by 296
“Its reaction with hydroxyl radicals (OH (cid:129) ) is virtually instantaneous, while it reacts only more slowly with H 2 O 2 and/or O 2 (cid:129) − (38) .”
Background
Antioxidants: Its medicinal and pharmacological applications
(2010) · African Journal of Pure and Applied Chemistry · doi:10.5897/ajpac.9000020 · Cited by 284
Inhibitory activity spectrum of reuterin produced by Lactobacillus reuteri against intestinal bacteria
Cleusix, V., Lacroix, C., Vollenweider, S., Duboux, M., & Blay, G. L. (2007) · BMC Microbiology · doi:10.1186/1471-2180-7-101 · Cited by 271
Staphylococcal response to oxidative stress
Gaupp, R., Ledala, N., & Somerville, G. A. (2012) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2012.00033 · Cited by 253
Biosynthesis and functions of bacillithiol, a major low-molecular-weight thiol in Bacilli
Gaballa, A., Newton, G., Antelmann, H., Parsonage, D., Upton, H. E., Rawat, M., Claiborne, A., Fahey, R. C., & Helmann, J. (2010) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1000928107 · Cited by 249
Self-citation
Disulfides as Redox Switches: From Molecular Mechanisms to Functional Significance
Wouters, M. A., Fan, S. W., & Haworth, N. L. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2510 · Cited by 238
An overview on glutathione in versus non-conventional yeasts
Penninckx, M. J. (2002) · FEMS Yeast Research · doi:10.1016/s1567-1356(02)00081-8 · Cited by 235
Microbial Mercury Methylation in Aquatic Environments: A Critical Review of Published Field and Laboratory Studies
Regnell, O., & Watras, C. J. (2018) · Environmental Science & Technology · doi:10.1021/acs.est.8b02709 · Cited by 248
The σ factors ofMycobacterium tuberculosis
Rodrigue, S., Provvedi, R., Jacques, P., Gaudreau, L. R., & Manganelli, R. (2006) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2006.00040.x · Cited by 228
Role of Glutathione in Winemaking: A Review
Kritzinger, E. C., Bauer, F. F., & du Toit, W. J. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf303665z · Cited by 226
Glutathione and Transition-Metal Homeostasis in Escherichia coli
Helbig, K., Bleuel, C., Krauss, G.-J., & Nies, D. H. (2008) · Journal of Bacteriology · doi:10.1128/jb.00271-08 · Cited by 218
Glutathione analogs in prokaryotes
Fahey, R. C. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.10.006 · Cited by 220
Self-citation
Glutaredoxins: roles in iron homeostasis
Rouhier, N., Couturier, J., Johnson, M. K., & Jacquot, J. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.08.005 · Cited by 216
Gene Knockout and Metabolome Analysis of Carnitine/Organic Cation Transporter OCTN1
Kato, Y., Kubo, Y., Iwata, D., Kato, S., Sudo, T., Sugiura, T., Kagaya, T., Wakayama, T., Hirayama, A., Sugimoto, M., et al. (2010) · Pharmaceutical Research · doi:10.1007/s11095-010-0076-z · Cited by 206
Mycothiol-Deficient Mycobacterium smegmatis Mutants Are Hypersensitive to Alkylating Agents, Free Radicals, and Antibiotics
Rawat, M., Newton, G. L., Ko, M., Martinez, G. J., Fahey, R. C., & Av‐Gay, Y. (2002) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.46.11.3348-3355.2002 · Cited by 196
Self-citation
Functions of elements in soil microorganisms
Hemkemeyer, M., Schwalb, S. A., Heinze, S., Joergensen, R. G., & Wichern, F. (2021) · Microbiological Research · doi:10.1016/j.micres.2021.126832 · Cited by 170
Mycothiol: synthesis, biosynthesis and biological functions of the major low molecular weight thiol in actinomycetes
Jothivasan, V. K., & Hamilton, C. J. (2008) · Natural Product Reports · doi:10.1039/b616489g · Cited by 155
Lateral gene transfer and parallel evolution in the history of glutathione biosynthesis genes
Copley, S. D., & Dhillon, J. K. (2002) · Genome biology · doi:10.1186/gb-2002-3-5-research0025 · Cited by 150
The evolution of development inStreptomycesanalysed by genome comparisons
Chater, K. F., & Chandra, G. (2006) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2006.00033.x · Cited by 143
Role of Ergothioneine in Microbial Physiology and Pathogenesis
Cumming, B. M., Chinta, K. C., Reddy, V. P., & Steyn, A. J. C. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7300 · Cited by 139
Ergothioneine oxidation in the protection against high-glucose induced endothelial senescence: Involvement of SIRT1 and SIRT6
D’Onofrio, N., Servillo, L., Giovane, A., Casale, R., Vitiello, M., Marfella, R., Paolisso, G., & Balestrieri, M. L. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.013 · Cited by 139
Sulfur metabolism in archaea reveals novel processes
Liu, Y., Beer, L. L., & Whitman, W. B. (2012) · Environmental Microbiology · doi:10.1111/j.1462-2920.2012.02783.x · Cited by 142
Sulfur and selenium antioxidants: Challenging radical scavenging mechanisms and developing structure–activity relationships based on metal binding
Zimmerman, M. T., Bayse, C. A., Ramoutar, R. R., & Brumaghim, J. L. (2014) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2014.12.020 · Cited by 132
Thiol cofactors for selenoenzymes and their synthetic mimics
Sarma, B. K., & Mugesh, G. (2008) · Organic & Biomolecular Chemistry · doi:10.1039/b716239a · Cited by 130
The Glutathione System: A Journey from Cyanobacteria to Higher Eukaryotes
Cassier‐Chauvat, C., Marceau, F., Farci, S., Ouchane, S., & Chauvat, F. (2023) · Antioxidants · doi:10.3390/antiox12061199 · Cited by 127
A thermophilic bacterial origin and subsequent constraints by redox, light and salinity on the evolution of the microbial mercuric reductase
Barkay, T., Kritee, K., Boyd, E. S., & Geesey, G. G. (2010) · Environmental Microbiology · doi:10.1111/j.1462-2920.2010.02260.x · Cited by 125
The Role of Bacillithiol in Gram-Positive Firmicutes
Chandrangsu, P., Loi, V. V., Antelmann, H., & Helmann, J. D. (2018) · Antioxidants & Redox Signaling · doi:10.1089/ars.2017.7057 · Cited by 120
Bioinformatic and Biochemical Characterizations of C–S Bond Formation and Cleavage Enzymes in the Fungus Neurospora crassa Ergothioneine Biosynthetic Pathway
Hu, W. J., Song, H., Her, A. S., Bak, D. W., Naowarojna, N., Elliott, S. J., Li, Q., Chen, X., & Liu, P. (2014) · Organic Letters · doi:10.1021/ol502596z · Cited by 118
Cadmium Toxicity in Glutathione Mutants ofEscherichia coli
Helbig, K., Große, C., & Nies, D. H. (2008) · Journal of Bacteriology · doi:10.1128/jb.00272-08 · Cited by 113
Bacillithiol, a New Player in Bacterial Redox Homeostasis
Helmann, J. D. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3562 · Cited by 113
Amidoligases with ATP-grasp, glutamine synthetase-like and acetyltransferase-like domains: synthesis of novel metabolites and peptide modifications of proteins
Iyer, L. M., Abhiman, S., Burroughs, A. M., & Aravind, L. (2009) · Molecular BioSystems · doi:10.1039/b917682a · Cited by 108
Mycothiol-dependent proteins in actinomycetes
Rawat, M., & Av‐Gay, Y. (2007) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2006.00062.x · Cited by 103
Production of ergothioneine by Methylobacterium species
Alamgir, K. M., Masuda, S., Fujitani, Y., Fukuda, F., & Tani, A. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.01185 · Cited by 100
Arabidopsis glutathione reductase 2 is indispensable in plastids, while mitochondrial glutathione is safeguarded by additional reduction and transport systems
Marty, L., Bausewein, D., Müller, C., Bangash, S. A. K., Moseler, A., Schwarzländer, M., Müller‐Schüssele, S. J., Zechmann, B., Riondet, C., Balk, J., et al. (2019) · New Phytologist · doi:10.1111/nph.16086 · Cited by 101
The Mycobacterium tuberculosis ino1 gene is essential for growth and virulence
Movahedzadeh, F., Smith, D. A., Norman, R. A., Dinadayala, P., Murray‐Rust, J., Russell, D. G., Kendall, S. L., Rison, S. C. G., McAlister, M. S. B., Bancroft, G. J., et al. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03900.x · Cited by 96
Relationship between Extracellular Low-Molecular-Weight Thiols and Mercury Species in Natural Lake Periphytic Biofilms
Leclerc, M., Planas, D., & Amyot, M. (2015) · Environmental Science & Technology · doi:10.1021/es505952x · Cited by 95
An uncommon redox behavior sheds light on the cellular antioxidant properties of ergothioneine
Servillo, L., Castaldo, D., Casale, R., D’Onofrio, N., Giovane, A., Cautela, D., & Balestrieri, M. L. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.11.017 · Cited by 93
Oxidative stress triggers thiol oxidation in the glyceraldehyde‐3‐phosphate dehydrogenase of Staphylococcus aureus
Weber, H., Engelmann, S., Becher, D., & Hecker, M. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.03971.x · Cited by 93
Some lessons fromRickettsiagenomics
Renesto, P., Ogata, H., Audic, S., Claverie, J., & Raoult, D. (2004) · FEMS Microbiology Reviews · doi:10.1016/j.femsre.2004.09.002 · Cited by 91
Synthesis of silver nanoparticles using haloarchaeal isolate Halococcus salifodinae BK3
Srivastava, P., Braganca, J. M., Ramanan, S. R., & Kowshik, M. (2013) · Extremophiles · doi:10.1007/s00792-013-0563-3 · Cited by 89
Inactivation of the Antibacterial and Cytotoxic Properties of Silver Ions by Biologically Relevant Compounds
Mulley, G., Jenkins, A. T. A., & Waterfield, N. R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0094409 · Cited by 88
Activity of 7-methyljuglone derivatives against Mycobacterium tuberculosis and as subversive substrates for mycothiol disulfide reductase
Mahapatra, A., Mativandlela, S. P. N., Binneman, B., Fourie, P. B., Hamilton, C. J., Meyer, J. J. M., van der Kooy, F., Houghton, P. J., & Lall, N. (2007) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2007.08.064 · Cited by 88
Linking Microbial Activities and Low-Molecular-Weight Thiols to Hg Methylation in Biofilms and Periphyton from High-Altitude Tropical Lakes in the Bolivian Altiplano
Bouchet, S., Goñi‐Urriza, M., Monperrus, M., Guyoneaud, R., Fernandez, P., Heredia, C., Tessier, E., Gassie, C., Point, D., Guédron, S., et al. (2018) · Environmental Science & Technology · doi:10.1021/acs.est.8b01885 · Cited by 86
Mechanisms of Metal Resistance and Homeostasis in Haloarchaea
Srivastava, P., & Kowshik, M. (2013) · Archaea · doi:10.1155/2013/732864 · Cited by 86
Identification and Characterization of Arsenite Methyltransferase from an Archaeon,Methanosarcina acetivoransC2A
Wang, P., Sun, G., & Zhu, Y. (2014) · Environmental Science & Technology · doi:10.1021/es503869k · Cited by 85
Inhibition and kinetics of mycobacterium tuberculosis and mycobacterium smegmatis mycothiol-S-conjugate amidase by natural product inhibitors
Nicholas, G. M., Eckman, L. L., Newton, G. L., Fahey, R. C., Ray, S., & Bewley, C. A. (2003) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(02)00345-0 · Cited by 84
Self-citation
Thioredoxin Reductase Is Essential for Thiol/Disulfide Redox Control and Oxidative Stress Survival of the Anaerobe Bacteroides fragilis
Rocha, E. R., Tzianabos, A. O., & Smith, C. J. (2007) · Journal of Bacteriology · doi:10.1128/jb.00714-07 · Cited by 81
The Antiaging Activity of Ergothioneine in UVA-Irradiated Human Dermal Fibroblasts via the Inhibition of the AP-1 Pathway and the Activation of Nrf2-Mediated Antioxidant Genes
Hseu, Y.-C., Vudhya Gowrisankar, Y., Chen, X.-Z., Yang, Y.-C., & Yang, H.-L. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/2576823 · Cited by 81
Oxygen intervention in the regulation of gene expression: the photosynthetic bacterial paradigm
Zeilstra-Ryalls, J. H., & Kaplan, S. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-3242-1 · Cited by 79
Mini-Review: Ergothioneine and Ovothiol Biosyntheses, an Unprecedented Trans-Sulfur Strategy in Natural Product Biosynthesis
Naowarojna, N., Cheng, R., Chen, L., Quill, M., Xu, M., Zhao, C., & Liu, P. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00239 · Cited by 76
Synthesis of Natural Product-Inspired Inhibitors of Mycobacterium tuberculosis Mycothiol-Associated Enzymes: The First Inhibitors of GlcNAc-Ins Deacetylase
Metaferia, B. B., Fetterolf, B., Shahzad‐ul‐Hussan, S., Moravec, M. D., Smith, J. A., Ray, S., Gutierrez‐Lugo, M., & Bewley, C. A. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm070669h · Cited by 74
Changes of global gene expression and secondary metabolite accumulation during light-dependent Aspergillus nidulans development
Bayram, Ö., Feussner, K., Dumkow, M., Herrfurth, C., Feußner, I., & Braus, G. H. (2016) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2016.01.004 · Cited by 71
Functional Studies of Multiple Thioredoxins from Mycobacterium tuberculosis
Akif, M., Khare, G., Tyagi, A. K., Mande, S. C., & Sardesai, A. A. (2008) · Journal of Bacteriology · doi:10.1128/jb.00159-08 · Cited by 71
Synthesis, characterization, and DFT studies of thione and selone Cu(i) complexes with variable coordination geometries
Kimani, M. M., Bayse, C. A., & Brumaghim, J. L. (2011) · Dalton Transactions · doi:10.1039/c1dt10104h · Cited by 70
TiO2 nanoparticles cause cell damage independent of apoptosis and autophagy by impairing the ROS-scavenging system in Pichia pastoris
Liu, Z., Zhang, M., Han, X., Xu, H., Zhang, B., Yu, Q., & Li, M. (2016) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2016.03.029 · Cited by 69
Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N‐acetyltransferases
Vetting, M. W., Roderick, S. L., Yu, M. C., & Blanchard, J. S. (2003) · Protein Science · doi:10.1110/ps.03153703 · Cited by 69
Methanogenic Inhibition by Arsenic Compounds
Sierra‐Álvarez, R., Cortinas, I., Yenal, U., & Field, J. A. (2004) · Applied and Environmental Microbiology · doi:10.1128/aem.70.9.5688-5691.2004 · Cited by 69
Metabolite Identification in Synechococcus sp. PCC 7002 Using Untargeted Stable Isotope Assisted Metabolite Profiling
Baran, R., Bowen, B. P., Bouskill, N., Brodie, E., Yannone, S. M., & Northen, T. R. (2010) · Analytical Chemistry · doi:10.1021/ac1020112 · Cited by 69
Metabolite profile of koji amazake and its lactic acid fermentation product by Lactobacillus sakei UONUMA
Oguro, Y., Nishiwaki, T., Shinada, R., Kobayashi, K., & Kurahashi, A. (2017) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2017.03.011 · Cited by 68
Sigma Factors: Key Molecules in Mycobacterium tuberculosis Physiology and Virulence
Manganelli, R. (2014) · Microbiology Spectrum · doi:10.1128/microbiolspec.mgm2-0007-2013 · Cited by 67
Transcriptome Profiling of Shewanella oneidensis Gene Expression following Exposure to Acidic and Alkaline pH
Leaphart, A. B., Thompson, D. K., Huang, K. H., Alm, E. J., Wan, X., Arkin, A. P., Brown, S. D., Wu, L., Yan, T., Liu, X., et al. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.4.1633-1642.2006 · Cited by 67
Bromotyrosine-Derived Natural and Synthetic Products as Inhibitors of Mycothiol-S-Conjugate Amidase
Nicholas, G. M., Eckman, L. L., Ray, S., Hughes, R. O., Pfefferkorn, J. A., Barluenga, S., Nicolaou, K. C., & Bewley, C. A. (2002) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(02)00385-2 · Cited by 66
Impairment of the carnitine/organic cation transporter 1–ergothioneine axis is mediated by intestinal transporter dysfunction in chronic kidney disease
Shinozaki, Y., Furuichi, K., Toyama, T., Kitajima, S., Hara, A., Iwata, Y., Sakai, N., Shimizu, M., Kaneko, S., Isozumi, N., et al. (2017) · Kidney International · doi:10.1016/j.kint.2017.04.032 · Cited by 66
Characterization of hemin-binding protein 35 (HBP35) in Porphyromonas gingivalis: its cellular distribution, thioredoxin activity and role in heme utilization
Shoji, M., Shibata, Y., Shiroza, T., Yukitake, H., Peng, B. H., Chen, Y., Sato, K., Naito, M., Abiko, Y., Reynolds, E. C., et al. (2010) · BMC Microbiology · doi:10.1186/1471-2180-10-152 · Cited by 65
Oxidation of Hg(0) to Hg(II) by diverse anaerobic bacteria
Colombo, M. J., Ha, J., Reinfelder, J. R., Barkay, T., & Yee, N. (2013) · Chemical Geology · doi:10.1016/j.chemgeo.2013.11.020 · Cited by 63
Redox Regulation in Bacillus subtilis: The Bacilliredoxins BrxA(YphP) and BrxB(YqiW) Function in De-Bacillithiolation of S-Bacillithiolated OhrR and MetE
Gaballa, A., Bùi, C. L. K., Roberts, A., Becher, D., Hamilton, C., Antelmann, H., & Helmann, J. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5327 · Cited by 62
Discovery of sulfated metabolites in mycobacteria with a genetic and mass spectrometric approach
Mougous, J. D., Leavell, M. D., Senaratne, R. H., Leigh, C. D., Williams, S. J., Riley, L. W., Leary, J. A., & Bertozzi, C. R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252514899 · Cited by 62
Dichloromethane-degrading bacteria in the genomic age
Muller, E. E. L., Bringel, F., & Vuilleumier, S. (2011) · Research in Microbiology · doi:10.1016/j.resmic.2011.01.008 · Cited by 61
Coenzyme A Biosynthesis and Enzymology
Strauss, E. (2010) · Elsevier eBooks · doi:10.1016/b978-008045382-8.00141-6 · Cited by 60
Regioselectivity of the Oxidative C–S Bond Formation in Ergothioneine and Ovothiol Biosyntheses
Song, H., Leninger, M., Lee, N., & Liu, P. (2013) · Organic Letters · doi:10.1021/ol402275t · Cited by 60
Comparative genomics of the oxidative stress response in bioleaching microorganisms
Cárdenas, J. P., Moya, F., Covarrubias, P. C., Shmaryahu, A., Levicán, G. J., Holmes, D. S., & Quatrini, R. (2012) · Hydrometallurgy · doi:10.1016/j.hydromet.2012.07.014 · Cited by 59
Structure of the Type III Pantothenate Kinase from Bacillus anthracis at 2.0 Å Resolution: Implications for Coenzyme A-Dependent Redox Biology,
Nicely, N. I., Parsonage, D., Paige, C., Newton, G. L., Fahey, R. C., Leonardi, R., Jackowski, S., Mallett, T. C., & Claiborne, A. (2007) · Biochemistry · doi:10.1021/bi062299p · Cited by 59
Self-citation
An insight into the mechanisms of homeostasis in extremophiles
Somayaji, A., Dhanjal, C. R., Lingamsetty, R., Vinayagam, R., Selvaraj, R., Varadavenkatesan, T., & Govarthanan, M. (2022) · Microbiological Research · doi:10.1016/j.micres.2022.127115 · Cited by 59
Novel precursor substrates for polythioesters (PTE) and limits of PTE biosynthesis inRalstonia eutropha
Lütke‐Eversloh, T., & Steinbüchel, A. (2003) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(03)00185-x · Cited by 57
Mechanism of Sulfoxidation and C–S Bond Formation Involved in the Biosynthesis of Ergothioneine Catalyzed by Ergothioneine Synthase (EgtB)
Tian, G., Su, H., & Liu, Y. (2018) · ACS Catalysis · doi:10.1021/acscatal.8b01473 · Cited by 55
Pangenomic comparison of globally distributed Poribacteria associated with sponge hosts and marine particles
Podell, S. B., Blanton, J. M., Neu, A. T., Agarwal, V., Biggs, J. S., Moore, B. S., & Allen, E. E. (2018) · The ISME Journal · doi:10.1038/s41396-018-0292-9 · Cited by 55
Mechanistic studies of a novel C-S lyase in ergothioneine biosynthesis: the involvement of a sulfenic acid intermediate
Song, H., Hu, W. J., Naowarojna, N., Her, A. S., Wang, S., Desai, R. N., Li, Q., Chen, X., & Liu, P. (2015) · Scientific Reports · doi:10.1038/srep11870 · Cited by 55
Investigating the copper coordination, electrochemistry, and Cu(ii) reduction kinetics of biologically relevant selone and thione compounds
Kimani, M. M., Wang, H. C., & Brumaghim, J. L. (2012) · Dalton Transactions · doi:10.1039/c2dt11731b · Cited by 54
Use of a Tyrosine Analogue To Modulate the Two Activities of a Nonheme Iron Enzyme OvoA in Ovothiol Biosynthesis, Cysteine Oxidation versus Oxidative C–S Bond Formation
Chen, L., Naowarojna, N., Song, H., Wang, S., Wang, J., Deng, Z., Zhao, C., & Liu, P. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.7b13628 · Cited by 54
Glutathione synthetase homologs encode α- l -glutamate ligases for methanogenic coenzyme F 420 and tetrahydrosarcinapterin biosyntheses
Li, H., Xu, H., Graham, D. E., & White, R. H. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1733391100 · Cited by 54
Total Synthesis and Proof of Structure of Mycothiol Bimane
Nicholas, G. M., Kováč, P., & Bewley, C. A. (2002) · Journal of the American Chemical Society · doi:10.1021/ja017891a · Cited by 54

Authors: Fahey, R. C.
Affiliations: University of California San Diego (US)
Corresponding author: Fahey, Robert C.
Venue: Annual Review of Microbiology
Publisher: Annual Reviews
Published: 2001-10
Volume: 55
Issue: 1
Pages: 333-356
ISSN: 0066-4227 (ISSN-L)
1545-3251
DOI: 10.1146/annurev.micro.55.1.333
OpenAlex: W2146918483
Cited by: 266
References: 133
Citations by year: 2026: 4 · 2025: 3 · 2024: 8 · 2023: 9 · 2022: 10 · 2021: 9 · 2020: 11 · 2019: 9 · 2018: 15 · 2017: 9 · 2016: 11 · 2015: 10 · 2014: 18 · 2013: 14 · 2012: 17
FWCI: 1.02
Type: journal article
Language: en
Open access: closed
Locations: Annual Review of Microbiology (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of Allergy and Infectious Diseases (AI 49174)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
Keywords: glutathione, purple sulfur bacteria, sulfide metabolism, coenzyme M, coenzyme B, methanogenic archaea, methane production, halobacteria, gamma-glutamylcysteine, mycothiol, actinomycetes, ergothioneine, antioxidant defense
MeSH terms: Cysteine, Disaccharides, Ergothioneine, Glutathione, Glycopeptides, Inositol, Models, Chemical, Phosphothreonine, Prokaryotic Cells, Pyrazoles, Sulfhydryl Compounds, Mesna

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Novel Thiols of Prokaryotes

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks