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

Flagged first, then by citations

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

Items 101–200 of 268

Ergothioneine production using Methylobacterium species, yeast, and fungi
Fujitani, Y., Alamgir, K. M., & Tani, A. (2018) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2018.05.021 · Cited by 53
Ergothioneine mitigates cisplatin-evoked nephrotoxicity via targeting Nrf2, NF-κB, and apoptotic signaling and inhibiting γ-glutamyl transpeptidase
Salama, S. A., Abd‐Allah, G. M., Mohamadin, A. M., Elshafey, M. M., & Gad, H. S. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119572 · Cited by 53
Metal Toxicity and Resistance in Plants and Microorganisms in Terrestrial Ecosystems
Narendrula-Kotha, R., Thériault, G., Mehes-Smith, M., Kalubi, K. N., & Nkongolo, K. K. C. (2019) · Reviews of Environmental Contamination and Toxicology · doi:10.1007/398_2018_22 · Cited by 54
An NADH-Dependent Bacterial Thioredoxin Reductase-like Protein in Conjunction with a Glutaredoxin Homologue Form a Unique Peroxiredoxin (AhpC) Reducing System in Clostridium pasteurianum
Reynolds, C. M., Meyer, J., & Poole, L. B. (2002) · Biochemistry · doi:10.1021/bi011802p · Cited by 53
Yap1-Regulated Glutathione Redox System Curtails Accumulation of Formaldehyde and Reactive Oxygen Species in Methanol Metabolism of Pichia pastoris
Yano, T., Takigami, E., Yurimoto, H., & Sakai, Y. (2009) · Eukaryotic Cell · doi:10.1128/ec.00007-09 · Cited by 52
The critical role of S‐lactoylglutathione formation during methylglyoxal detoxification in Escherichia coli
Ozyamak, E., Black, S. S., Walker, C. A., MacLean, M. J., Bartlett, W., Miller, S. N., & Booth, I. R. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07426.x · Cited by 51
Cysteine Oxidation Reactions Catalyzed by a Mononuclear Non-heme Iron Enzyme (OvoA) in Ovothiol Biosynthesis
Song, H., Her, A. S., Raso, F., Zhen, Z.-B., Huo, Y., & Liu, P. (2014) · Organic Letters · doi:10.1021/ol5005438 · Cited by 50
Increase in the Protein-Bound Form of Glutathione in Human Blood after the Oral Administration of Glutathione
Park, E. Y., Shimura, N., Konishi, T., Sauchi, Y., Wada, S., Aoi, W., Nakamura, Y. K., & Sato, K. (2014) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf501338z · Cited by 49
The Hyperthermophilic Bacterium Aquifex aeolicus
Guiral, M., Prunetti, L., Aussignargues, C., Ciaccafava, A., Infossi, P., Ilbert, M., Lojou, É., & Giudici‐Orticoni, M. (2012) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/b978-0-12-394423-8.00004-4 · Cited by 48
Snapshots of C-S Cleavage in Egt2 Reveals Substrate Specificity and Reaction Mechanism
Irani, S., Naowarojna, N., Tang, Y., Kathuria, K. R., Wang, S., Dhembi, A., Lee, N., Yan, W., Lyu, H., Costello, C. E., et al. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.02.002 · Cited by 48
Modulating NF‐κB, MAPK, and PI3K/AKT signaling by ergothioneine attenuates iron overload‐induced hepatocellular injury in rats
Salama, S. A., & Omar, H. A. (2021) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.22729 · Cited by 46
Shortcut to Mycothiol Analogues
Knapp, S., González, S., Myers, D. S., Eckman, L. L., & Bewley, C. A. (2002) · Organic Letters · doi:10.1021/ol0269796 · Cited by 45
Molecular characterization of the thioredoxin system from M ethanosarcina acetivorans
McCarver, A. C., & Lessner, D. J. (2014) · FEBS Journal · doi:10.1111/febs.12964 · Cited by 44
Rv2466c Mediates the Activation of TP053 To Kill Replicating and Non-replicating Mycobacterium tuberculosis
Albesa-Jové, D., Chiarelli, L. R., Makarov, V., Pasca, M. R., Urresti, S., Mori, G., Salina, E. G., Vocat, A., Comino, N., Mohorko, E., et al. (2014) · ACS Chemical Biology · doi:10.1021/cb500149m · Cited by 45
Structure of Coenzyme A−Disulfide Reductase from Staphylococcus aureus at 1.54 Å Resolution,
Mallett, T. C., Wallen, J. R., Karplus, P. A., Sakai, H., Tomitake Tsukihara, A., & Claiborne, A. (2006) · Biochemistry · doi:10.1021/bi061139a · Cited by 44
Evaluation of photolyase (Photosome®) repair activity in human keratinocytes after a single dose of ultraviolet B irradiation using the comet assay
Decome, L., Méo, M. D., Geffard, A., Doucet, O., Duménil, G., & Botta, A. (2005) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2004.11.022 · Cited by 43
Synthesis of Bacillithiol and the Catalytic Selectivity of FosB-Type Fosfomycin Resistance Proteins
Lamers, A. P., Keithly, M. E., Kim, K., Cook, P. D., Stec, D. F., Hines, K. M., Sulikowski, G. A., & Armstrong, R. N. (2012) · Organic Letters · doi:10.1021/ol302327t · Cited by 42
Corynebacterium glutamicum survives arsenic stress with arsenate reductases coupled to two distinct redox mechanisms
Villadangos, A. F., Belle, K. V., Wahni, K., Dufe, V. T., Freitas, S., Nur, H., Galan, S. D., Gil, J. A., Collet, J., Mateos, L. M., et al. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07882.x · Cited by 42
Hg(II) sequestration and protection by the MerR metal-binding domain (MBD)
Qin, J., Song, L., Brim, H., Daly, M. J., & Summers, A. O. (2006) · Microbiology · doi:10.1099/mic.0.28474-0 · Cited by 42
Discovery and characterization of a Coenzyme A disulfide reductase from Pyrococcus horikoshii
Harris, D. R., Ward, D. E., Feasel, J. M., Lancaster, K. M., Murphy, R. D., Mallett, T. C., & Crane, E. J. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04555.x · Cited by 41
In Vitro Reconstitution of the Remaining Steps in Ovothiol A Biosynthesis: C–S Lyase and Methyltransferase Reactions
Naowarojna, N., Huang, P., Cai, Y., Song, H., Wu, L., Cheng, R., Li, Y., Wang, S., Lyu, H., Zhang, L., et al. (2018) · Organic Letters · doi:10.1021/acs.orglett.8b02332 · Cited by 40
The Physiology and Genetics of Oxidative Stress in Mycobacteria
Cumming, B. M., Lamprecht, D. A., Wells, R. M., Saini, V., Mazorodze, J. H., & Steyn, A. J. C. (2014) · Microbiology Spectrum · doi:10.1128/microbiolspec.mgm2-0019-2013 · Cited by 42
Palladium-Catalyzed Dehydrative Cross-Coupling of Allylic Alcohols and N-Heterocycles Promoted by a Bicyclic Bridgehead Phosphoramidite Ligand and an Acid Additive
Kang, K., Kim, J., Lee, A., Kim, W. Y., & Kim, H. (2016) · Organic Letters · doi:10.1021/acs.orglett.6b00001 · Cited by 39
Contributions of MS metabolomics to gilthead sea bream (Sparus aurata) nutrition. Serum fingerprinting of fish fed low fish meal and fish oil diets
Gil‐Solsona, R., Calduch-Giner, J. À., Nácher‐Mestre, J., Lacalle-Bergeron, L., Sancho, J. V., Hernández, F. J., & Pérez‐Sánchez, J. (2018) · Aquaculture · doi:10.1016/j.aquaculture.2018.08.080 · Cited by 39
Introduction to approaches and tools for the evaluation of protein cysteine oxidation
Poole, L. B., Furdui, C. M., & King, S. B. (2020) · Essays in Biochemistry · doi:10.1042/ebc20190050 · Cited by 39
Thiol/Disulfide Redox Switches in the Regulation of Heme Binding to Proteins
Ragsdale, S. W., & Li, Y. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3436 · Cited by 39
Broad specificity AhpC-like peroxiredoxin and its thioredoxin reductant in the sparse antioxidant defense system of Treponema pallidum
Parsonage, D., Desrosiers, D. C., Hazlett, K. R. O., Sun, Y., Nelson, K. J., Cox, D. L., Radolf, J. D., & Poole, L. B. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910057107 · Cited by 38
Integrated stress response of E scherichia coli to methylglyoxal: transcriptional readthrough from the nemRA operon enhances protection through increased expression of glyoxalase I
Ozyamak, E., de Almeida, C., de Moura, A. P. S., Miller, S., & Booth, I. R. (2013) · Molecular Microbiology · doi:10.1111/mmi.12234 · Cited by 38
Involvement of the oscA gene in the sulphur starvation response and in Cr(VI) resistance in Pseudomonas corrugata 28
Viti, C., Decorosi, F., Mini, A., Tatti, E., & Giovannetti, L. (2008) · Microbiology · doi:10.1099/mic.0.021873-0 · Cited by 37
High-resolution structures of oxidized and reduced thioredoxin reductase fromHelicobacter pylori
Gustafsson, T. N., Sandalova, T., Lu, J., Holmgren, A., & Schneider, G. (2007) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444907026303 · Cited by 36
Low-molecular-weight thiol transferases in redox regulation and antioxidant defence
Tossounian, M., Zhao, Y., Yu, B. Y. K., Markey, S. A., Malanchuk, O., Zhu, Y., Cain, A., & Gout, I. T. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103094 · Cited by 35
Crystal Structure of the Ergothioneine Sulfoxide Synthase from Candidatus Chloracidobacterium thermophilum and Structure-Guided Engineering To Modulate Its Substrate Selectivity
Naowarojna, N., Irani, S., Hu, W., Cheng, R., Zhang, L., Li, X., Chen, J., Zhang, Y., & Liu, P. (2019) · ACS Catalysis · doi:10.1021/acscatal.9b02054 · Cited by 35
Design and synthesis of substrate-mimic inhibitors of mycothiol-S-conjugate amidase from Mycobacterium tuberculosis
Metaferia, B. B., Ray, S., Smith, J. A., & Bewley, C. A. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.10.031 · Cited by 33
Fungi's treasure in cosmeceuticals-a comprehensive chemical approach
Mukherjee, A., Das, S., Chakraborty, D., Pal, N., & Das, N. (2024) · South African Journal of Botany · doi:10.1016/j.sajb.2024.01.036 · Cited by 33
The antibacterial prodrug activator Rv2466c is a mycothiol-dependent reductase in the oxidative stress response of Mycobacterium tuberculosis
Rosado, L. A., Wahni, K., Degiacomi, G., Pedre, B., Young, D., la Rubia, A. G. D., Boldrin, F., Martens, E., Marcos-Pascual, L., Sancho‐Vaello, E., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.797837 · Cited by 32
Single-Step Replacement of an Unreactive C–H Bond by a C–S Bond Using Polysulfide as the Direct Sulfur Source in the Anaerobic Ergothioneine Biosynthesis
Cheng, R., Wu, L., Lai, R., Peng, C., Naowarojna, N., Hu, W., Li, X., Whelan, S. A., Lee, N., Lopez, J., et al. (2020) · ACS Catalysis · doi:10.1021/acscatal.0c01809 · Cited by 32
The Unusual Bifunctional Catalysis of Epimerization and Desaturation by Carbapenem Synthase
Topf, M., Sandala, G. M., Smith, D. M., Schofield, C. J., Easton, C. J., & Radom, L. (2004) · Journal of the American Chemical Society · doi:10.1021/ja047899v · Cited by 32
Reaching for Mechanistic Consensus Across Life Kingdoms: Structure and Insights into Catalysis of the myo-Inositol-1-phosphate Synthase (mIPS) from Archaeoglobus fulgidus,
Stieglitz, K. A., Yang, H., Roberts, M. F., & Stec, B. (2004) · Biochemistry · doi:10.1021/bi048267o · Cited by 32
Genomic Comparison, Phylogeny and Taxonomic Reevaluation of the Ectothiorhodospiraceae and Description of Halorhodospiraceae fam. nov. and Halochlorospira gen. nov.
Imhoff, J. F., Kyndt, J. A., & Meyer, T. E. (2022) · Microorganisms · doi:10.3390/microorganisms10020295 · Cited by 31
Coordination Switch Drives Selective C−S Bond Formation by the Non‐Heme Sulfoxide Synthases**
Wu, P., Gu, Y., Liao, L., Wu, Y., Jin, J., Wang, Z., Zhou, J., Shaik, S. S., & Wang, B. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202214235 · Cited by 30
Crystal structure of the conserved protein TT1542 from Thermus thermophilus HB8
Handa, N., Terada, T., Kamewari, Y., Hamana, H., Tame, J. R. H., Park, S., Kinoshita, K., Ota, M., Nakamura, H., Kuramitsu, S., et al. (2003) · Protein Science · doi:10.1110/gad.03104003 · Cited by 30
Characterization of a Thioredoxin-Thioredoxin Reductase System from the Hyperthermophilic BacteriumThermotoga maritima
Yang, X., & Ma, K. (2010) · Journal of Bacteriology · doi:10.1128/jb.01035-09 · Cited by 29
Determination of coenzyme A levels in Pyrococcus furiosus and other Archaea: implications for a general role for coenzyme A in thermophiles
Hummel, C. S., Lancaster, K. M., & Crane, E. J. (2005) · FEMS Microbiology Letters · doi:10.1016/j.femsle.2005.09.004 · Cited by 29
Survival of Escherichia coli Cells on Solid Copper Surfaces Is Increased by Glutathione
Große, C., Schleuder, G., Schmole, C., & Nies, D. H. (2014) · Applied and Environmental Microbiology · doi:10.1128/aem.02842-14 · Cited by 29
An overview on glutathione inSaccharomycesversus non-conventional yeasts
Penninckx, M. J. (2002) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2002.tb00098.x · Cited by 29
Comparative genomic analysis between Corynebacterium pseudotuberculosis strains isolated from buffalo
Viana, M. V. C., Figueiredo, H. C. P., Ramos, R. T. J., Guimarães, L. C., Pereira, F. L., Dorella, F. A., Selim, S. A. K., Salaheldean, M., Silva, A., Wattam, A. R., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0176347 · Cited by 27
Strong poison revisited
Prince, R. C., Gailer, J., Gunson, D. E., Turner, R. J., George, G. N., & Pickering, I. J. (2007) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2007.06.008 · Cited by 27
The pleiotropic transcriptional response of Mycobacterium tuberculosis to vitamin C is robust and overlaps with the bacterial response to multiple intracellular stresses
Sikri, K., Kumari, P., Tyagi, J. S., Nandi, M., Taneja, N. K., & Batra, S. D. (2015) · Microbiology · doi:10.1099/mic.0.000049 · Cited by 26
Novel l -Cysteine-Dependent Maleylpyruvate Isomerase in the Gentisate Pathway of Paenibacillus sp. Strain NyZ101
Liu, T., & Zhou, N. (2012) · Journal of Bacteriology · doi:10.1128/jb.00050-12 · Cited by 25
Subcellular distribution of glutathione and cysteine in cyanobacteria
Zechmann, B., Tomašić, A., Horvat, L. L., & Fulgosi, H. (2010) · PROTOPLASMA · doi:10.1007/s00709-010-0126-8 · Cited by 25
Functional Characterization of Corynebacterium glutamicum Mycothiol S-Conjugate Amidase
Si, M., Long, M., Chaudhry, M. T., Xu, Y., Zhang, P., Zhang, L., & Shen, X. (2014) · PLoS ONE · doi:10.1371/journal.pone.0115075 · Cited by 24
Identification and Characterization of gshA , a Gene Encoding the Glutamate-Cysteine Ligase in the Halophilic Archaeon Haloferax volcanii
Malki, L., Yanku, M., Borovok, I., Cohen, G., Mevarech, M., & Aharonowitz, Y. (2009) · Journal of Bacteriology · doi:10.1128/jb.00297-09 · Cited by 24
Mass spectrometry-based assay for the rapid detection of thiol-containing natural products
Capehart, S. L., & Carlson, E. E. (2016) · Chemical Communications · doi:10.1039/c6cc07111b · Cited by 26
Ergothioneine improves myocardial remodeling and heart function after acute myocardial infarction via S-glutathionylation through the NF-ĸB dependent Wnt5a-sFlt-1 pathway
Duan, R., Pan, H., Li, D., Liao, S., & Han, B. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.175759 · Cited by 23
IP6 (Inositol Hexaphosphate) as a Signaling Molecule
Shamsuddin, A. K., & Bose, S. (2012) · Current Signal Transduction Therapy · doi:10.2174/157436212802481628 · Cited by 23
Implications for an Imidazole-2-yl Carbene Intermediate in the Rhodanase-Catalyzed C–S Bond Formation Reaction of Anaerobic Ergothioneine Biosynthesis
Cheng, R., Lai, R., Peng, C., Lopez, J., Li, Z., Naowarojna, N., Li, K., Wong, C., Lee, N., Whelan, S. A., et al. (2021) · ACS Catalysis · doi:10.1021/acscatal.0c04886 · Cited by 23
An initial characterization of the mercury resistance (mer) system of the thermophilic bacterium Thermus thermophilus HB27
Wang, Y., Freedman, Z. B., Lu‐Irving, P., Kaletsky, R. L., & Barkay, T. (2008) · FEMS Microbiology Ecology · doi:10.1111/j.1574-6941.2008.00603.x · Cited by 22
Varietal Aromas of Sauvignon Blanc: Impact of Oxidation and Antioxidants Used in Winemaking
Tsai, P.-C., Araújo, L. D., & Tian, B. (2022) · Fermentation · doi:10.3390/fermentation8120686 · Cited by 23
Expanding the paradigm of thiol redox in the thermophilic root of life
Heinemann, J. V., Hamerly, T., Maaty, W. S. A., Movahed, N., Steffens, J. D., Reeves, B. D., Hilmer, J. K., Therien, J., Grieco, P. A., Peters, J. W., et al. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.08.009 · Cited by 21
Synthesis of 1-d- and 1-l-myo-inosityl 2-N-acetamido-2-deoxy-α-d-glucopyranoside establishes substrate specificity of the Mycobacterium tuberculosis enzyme AcGI deacetylase
Nicholas, G. M., Eckman, L. L., Kováč, P., Otero‐Quintero, S., & Bewley, C. A. (2003) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(03)00154-8 · Cited by 21
Mycothiol disulfide reductase: solid phase synthesis and evaluation of alternative substrate analogues
Stewart, M. J., Jothivasan, V. K., Rowan, A. S., Wagg, J., & Hamilton, C. J. (2007) · Organic & Biomolecular Chemistry · doi:10.1039/b716380k · Cited by 21
Importance and regulation of inositol biosynthesis during growth and differentiation of Streptomyces
Zhang, G., Tian, Y., Hu, K., Zhu, Y., Chater, K. F., Chi, F., Liu, G., & Tan, H. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.08000.x · Cited by 19
Quantification of L‐ergothioneine in whole blood by hydrophilic interaction ultra‐performance liquid chromatography and UV ‐detection
Sotgia, S., Zinellu, A., Pintus, G., Pinna, G. A., Deiana, L., & Carru, C. (2012) · Journal of Separation Science · doi:10.1002/jssc.201201016 · Cited by 19
Controlling Specific Growth Rate for Recombinant Protein Production by Pichia pastoris Under Oxidation Stress in Fed-batch Fermentation
Hu, R., Cui, R., Xu, Q., Lan, D., & Wang, Y. (2022) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-022-04022-3 · Cited by 18
Molecular Basis of Thioredoxin-Dependent Arsenic Transformation in Methanogenic Archaea
Liang, Y., Yan, Y., Shi, L., Wang, M., Yuan, X.-Z., Wang, S., Li, Y., & Yan, Z. (2024) · Environmental Science & Technology · doi:10.1021/acs.est.4c06611 · Cited by 18
Biochemical and Structural Characterization of OvoATh2: A Mononuclear Nonheme Iron Enzyme from Hydrogenimonas thermophila for Ovothiol Biosynthesis
Wang, X., Hu, S., Wang, J., Zhang, T., Ye, K., Wen, A., Zhu, G., Vegas, A. J., Zhang, L., Yan, W., et al. (2023) · ACS Catalysis · doi:10.1021/acscatal.3c04026 · Cited by 17
Gold nanoclusters exert antibacterial effects against gram-negative bacteria by targeting thiol-redox homeostasis
Meng, J., Gao, Y., Li, W., Wang, J., & Chen, X. (2021) · Talanta · doi:10.1016/j.talanta.2021.122618 · Cited by 17
Interplay of the intermolecular and intramolecular interactions in stabilizing the thione-based copper(I) complexes and their significance in protecting the biomolecules against metal-mediated oxidative damage
Chalana, A. K., Kumar, R., Karri, R., Jha, K. K., Kumar, B., & Roy, G. (2022) · Polyhedron · doi:10.1016/j.poly.2021.115647 · Cited by 16
Biochemical Origins of Lactaldehyde and Hydroxyacetone in Methanocaldococcus jannaschii
White, R. H. (2008) · Biochemistry · doi:10.1021/bi800069x · Cited by 16
Genetic and Proteomic Studies of Sulfur Oxidation in Chlorobium tepidum (syn. Chlorobaculum tepidum)
Chan, L., Morgan‐Kiss, R. M., & Hanson, T. E. (2008) · Advances in photosynthesis and respiration · doi:10.1007/978-1-4020-6863-8_18 · Cited by 16
Non-Heme Mono-Iron Enzymes: Co-Substrate-Independent Dioxygen Activation
Guo, Y., Chang, W., Li, J., & Davidson, M. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.14905-4 · Cited by 15
The Potassium Efflux System Kef: Bacterial Protection against Toxic Electrophilic Compounds
Rasmussen, T. (2023) · Membranes · doi:10.3390/membranes13050465 · Cited by 16
Structure and Substrate Specificity of the Pyrococcal Coenzyme A Disulfide Reductases/Polysulfide Reductases (CoADR/Psr): Implications for S0-Based Respiration and a Sulfur-Dependent Antioxidant System in Pyrococcus
Herwald, S. E., Liu, A. Y., Zhu, B. E., Sea, K. W., Lopez, K. M., Sazinsky, M. H., & Crane, E. J. (2013) · Biochemistry · doi:10.1021/bi3014399 · Cited by 15
The Significance of Glutathione Conjugation in Aflatoxin Metabolism
Ziglari, T., & Allameh, A. (2013) · InTech eBooks · doi:10.5772/52096 · Cited by 15
Inositol-1-phosphate synthetase mRNA as a new target for antisense inhibition of Mycobacterium tuberculosis
Li, Y., Chen, Z., Li, X., Zhang, H., Huang, Q., Zhang, Y., & Xu, S. (2007) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2006.12.019 · Cited by 14
The Methanosarcina acetivorans thioredoxin system activates DNA binding of the redox-sensitive transcriptional regulator MsvR
Sheehan, R. C., McCarver, A. C., Isom, C. E., Karr, E. A., & Lessner, D. J. (2015) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/s10295-015-1592-y · Cited by 14
The Type III Pantothenate Kinase Encoded by coaX Is Essential for Growth of Bacillus anthracis
Paige, C., Reid, S. D., Hanna, P. C., & Claiborne, A. (2008) · Journal of Bacteriology · doi:10.1128/jb.00860-08 · Cited by 14
Proteomic approach to enhance doxorubicin production in panK-integrated Streptomyces peucetius ATCC 27952
Song, E., Malla, S., Yang, Y., Lee, K., Kim, E. J., Lee, H. C., Sohng, J. K., Oh, M., & Kim, B. (2011) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/s10295-010-0903-6 · Cited by 13
Gene cloning and characterization of thiourocanate hydratase from Burkholderia sp. HME13
Muramatsu, H., 宮奥晴菜, Kurita, S., Matsuo, H., Kashiwagi, T., Kim, C.-S., Hayashi, M., Yamamoto, H., Kato, S.-I., & Nagata, S. (2019) · The Journal of Biochemistry · doi:10.1093/jb/mvz098 · Cited by 13
General Metabolism and Biochemical Pathways of Tubercle Bacilli
Wheeler, P. R., & Blanchard, J. S. (2004) · Wiley eBooks · doi:10.1128/9781555817657.ch20 · Cited by 13
Dynamics of Different Sulfur Forms in Natural Waters and Their Influence on the Redox State
Duca, G. G., Blonschi, V., Gladchi, V., & Travin, S. O. (2020) · American Journal of Physical Chemistry · doi:10.11648/j.ajpc.20200903.12 · Cited by 12
Measurement of glutathione in activated sludges
Dziurla, M.-A., Leroy, P., Strünkmann, G. W., Salhi, M., Lee, D. U., Camacho, P., Heinz, V., Müller, J., Paul, E., Ginestet, P., et al. (2003) · Water Research · doi:10.1016/j.watres.2003.08.028 · Cited by 12
Occurrence and biosynthesis of 3-mercaptopropionic acid inMethanocaldococcus jannaschii
Allen, K. D., & White, R. H. (2016) · FEMS Microbiology Letters · doi:10.1093/femsle/fnw217 · Cited by 12
Preparation and utilization of a reagent for the isolation and purification of low-molecular-mass thiols
Steenkamp, D. J., & VOGT, R. N. (2003) · Analytical Biochemistry · doi:10.1016/j.ab.2003.10.011 · Cited by 12
Turnover-Dependent Covalent Inactivation of Staphylococcus aureus Coenzyme A-Disulfide Reductase by Coenzyme A-Mimetics: Mechanistic and Structural Insights
Wallace, B. D., Edwards, J. S., Wallen, J. R., Moolman, W. J. A., van der Westhuyzen, R., Strauss, E., Redinbo, M. R., & Claiborne, A. (2012) · Biochemistry · doi:10.1021/bi301026c · Cited by 12
A glutaredoxin-fused thiol peroxidase acts as an important player in hydrogen peroxide detoxification in late-phased growth of Anabaena sp. PCC7120
Hong, S., Cha, M., & Kim, I.-H. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.04.006 · Cited by 12
Thiol-Activated DNA Damage by α-Bromo-2-cyclopentenone
Fekry, M. I., Price, N. E., Zang, H., Huang, C., Harmata, M. A., Brown, P., Daniels, J. S., & Gates, K. S. (2011) · Chemical Research in Toxicology · doi:10.1021/tx100282b · Cited by 11
Methanosarcina acetivorans utilizes a single NADPH-dependent thioredoxin system and contains additional thioredoxin homologues with distinct functions
McCarver, A. C., Lessner, F. H., Soroeta, J. M., & Lessner, D. J. (2016) · Microbiology · doi:10.1099/mic.0.000406 · Cited by 11
MdHAL3, a 4′-phosphopantothenoylcysteine decarboxylase, is involved in the salt tolerance of autotetraploid apple
Yang, S., Zhang, F., Wang, Y., Xue, H., Jiang, Q., Shi, J., Dai, H., Zhang, Z., Li, L., He, P., et al. (2020) · Plant Cell Reports · doi:10.1007/s00299-020-02576-2 · Cited by 10
Intra-molecular reactions as a new approach to investigate bio-radical reactivity: a case study of cysteine sulfinyl radicals
Durand, K. L., Ma, X., & Xia, Y. (2014) · The Analyst · doi:10.1039/c3an02307a · Cited by 10
Oxidative Stress Responses and Redox Signalling Mechanisms in Bacillus subtilis and Staphylococcus aureus
Antelmann, H. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-397169-2.00013-5 · Cited by 12
Non-heme iron enzyme-catalyzed complex transformations
Song, H., Naowarojna, N., Cheng, R., Lopez, J., & Liu, P. (2019) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.06.002 · Cited by 9
Non-Heme Mono-Iron Enzymes: Co-Substrate-Dependent Dioxygen Activation
Guo, Y., Chang, W., Li, J., & Davidson, M. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.14820-6 · Cited by 9
SCO3900, Co-Transcripted with Three Downstream Genes, Is Involved in the Differentiation of Streptomyces coelicolor
Zhang, G., Tian, Y., Hu, K., Chi, F., & Tan, H. (2009) · Current Microbiology · doi:10.1007/s00284-009-9536-2 · Cited by 9
Bacterial mechanisms of reversible protein S ‐thiolation: structural and mechanistic insights into mycoredoxins
Antelmann, H., & Hamilton, C. J. (2012) · Molecular Microbiology · doi:10.1111/mmi.12031 · Cited by 9
Structure-based identification of natural compound inhibitor against M. tuberculosis thioredoxin reductase: insight from molecular docking and dynamics simulation
Lata, S., & Akif, M. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1778530 · Cited by 9
Biosynthesis, Compartmentation and Cellular Functions of Glutathione in Plant Cells
Meyer, A. J., & Rausch, T. (2008) · Advances in photosynthesis and respiration · doi:10.1007/978-1-4020-6863-8_9 · Cited by 9
The Chalcogen Exchange: The Replacement of Oxygen with Sulfur and Selenium to Boost the Activity of Natural Products
Nasim, M. J., Ali, W., Júnior, E. N. D. S., Saleem, R. S. Z., Gaucher, C., Handzlik, J., Pedatella, S., & Jacob, C. (2025) · Sci · doi:10.3390/sci7020074 · Cited by 8
Bacillus subtilis YtpP and Thioredoxin A Are New Players in the Coenzyme-A-Mediated Defense Mechanism against Cellular Stress
Tossounian, M., Baczynska, M., Dalton, W., Peak‐Chew, S., Undzenas, K., Korza, G., Filonenko, V. V., Skehel, M. J., Setlow, P., & Gout, I. T. (2023) · Antioxidants · doi:10.3390/antiox12040938 · Cited by 8
Metabolic turnover of cysteine-related thiol compounds at environmentally relevant concentrations by Geobacter sulfurreducens
Gutensohn, M., Schaefer, J. K., Maas, T. J., Skyllberg, U., & Björn, E. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.1085214 · Cited by 9

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