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
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“ERG reacts fast with hydroxyl radicals, and its reaction with hydrogen peroxide and superoxide radical anion is somewhat slower (Fahey 2001).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Fahey 2001
Citations
Cites
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
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
Jocelyn, P. C. (1972) · Cited by 699
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
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
Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes
Newton, G. L., Arnold, K., Price, M. S., Sherrill, C., Delcardayre, S. B., Aharonowitz, Y., Cohen, G., Davies, J., Fahey, R. C., & Davis, C. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.7.1990-1995.1996 · Cited by 523
Self-citationOccurrence of glutathione in bacteria
Fahey, R. C., Brown, W., Adams, W. B., & Worsham, M. B. (1978) · Journal of Bacteriology · doi:10.1128/jb.133.3.1126-1129.1978 · Cited by 522
Self-citationUNUSUAL 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 508
Primordial Carbonylated Iron-Sulfur Compounds and the Synthesis of Pyruvate
Cody, G. D., Boctor, N. Z., Filley, T. R., Hazen, R. M., Scott, J. H., Sharma, A., & Yoder, H. S. (2000) · Science · doi:10.1126/science.289.5483.1337 · Cited by 441
Biosynthesis of dimethylarsine by methanobacterium
McBride, B. C., & WOLFE, R. S. (1971) · Biochemistry · doi:10.1021/bi00799a024 · Cited by 394
Fahey, R. C., & Newton, G. L. (1987) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(87)43016-4 · Cited by 380
Self-citationGlutathione : metabolism and physiological functions
Viña, J. (1990) · CRC Press eBooks · Cited by 377
The chemistry and biochemistry of the sulfhydryl group in amino acids, peptides, and proteins
Friedman, M. (1973) · Cited by 325
Kwon, B. S., Tan, K. B., Ni, J., Lee, Z. H., Kim, K. K., Kim, Y.-J., Wang, S., Gentz, R., Yu, G., Harrop, J., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.22.14272 · Cited by 303
Anaerobic respiration with elemental sulfur and with disulfides
Hedderich, R., Klimmek, O., Kröger, A., Dirmeier, R., Keller, M., & STETTER, K. O. (1998) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.1998.tb00376.x · Cited by 289
Direct evidence for secondary loss of mitochondria in Entamoeba histolytica.
Clark, C. G., & Roger, A. J. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.14.6518 · Cited by 283
Blueprint for a cell - the nature and origin of life
(1991) · Choice Reviews Online · doi:10.5860/choice.28-5078 · Cited by 273
The β-lactam antibiotics: past, present, and future
Demain, A. L., & Elander, R. P. (1999) · Antonie van Leeuwenhoek · doi:10.1023/a:1001738823146 · Cited by 256
Structure and Methylation of Coenzyme M (HSCH2CH2SO3)
Taylor, C. D., & WOLFE, R. S. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42403-4 · Cited by 256
The Enzymes of Glutathione Synthesis: γ‐Glutamylcysteine Synthetase
Griffith, O. W., & Mulcahy, R. (1999) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123195.ch7 · Cited by 254
The antioxidant action of ergothioneine
Akanmu, D., Cecchini, R., Aruoma, O. I., & Halliwell, B. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90158-f · Cited by 251
The final step in methane formation
ELLERMANN, J., Hedderich, R., Böcher, R., & Thauer, R. K. (1988) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1988.tb13941.x · Cited by 244
Heinen, W., & Lauwers, A. M. (1996) · Origins of life and evolution of the biosphere · doi:10.1007/bf01809852 · Cited by 236
Bacterial glutathione S-transferases: what are they good for?
Vuilleumier, S. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.5.1431-1441.1997 · Cited by 218
Glutathione and trypanothione in parasitic hydroperoxide metabolism
Flohé, L., Hecht, H., & Steinert, P. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00172-0 · Cited by 210
Hidalgo, E., Bollinger, J. M., Jr., Bradley, T. M., Walsh, C. T., & Demple, B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.36.20908 · Cited by 207
[32] Ergothioneine as antioxidant
Hartman, P. E. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)86124-e · Cited by 197
Entamoeba histolytica : a Eukaryote Without Glutathione Metabolism
Fahey, R. C., Newton, G. L., Arrick, B. A., Overdank-Bogart, T., & Aley, S. B. (1984) · Science · doi:10.1126/science.6322306 · Cited by 196
Self-citationAbken, H., Tietze, M., Brodersen, J., Bäumer, S., Beifuß, U., & Deppenmeier, U. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.8.2027-2032.1998 · Cited by 194
Huxtable, R. J. (1986) · Springer eBooks · doi:10.1007/978-1-4757-9438-0 · Cited by 191
Evolution of Glutathione Metabolism
Fahey, R. C., & Sundquist, A. R. (1991) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123102.ch1 · Cited by 183
Self-citationMetabolism and Functions of Glutathione in Micro-organisms
Penninckx, M. J., & Elskens, M. T. (1993) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/s0065-2911(08)60031-4 · Cited by 178
Newton, G. L., Av‐Gay, Y., & Fahey, R. C. (2000) · Biochemistry · doi:10.1021/bi000356n · Cited by 178
Self-citationRole for Ferredoxins in the Origin of Life and Biological Evolution
HALL, D. O., CAMMACK, R., & RAO, K. K. (1971) · Nature · doi:10.1038/233136a0 · Cited by 177
Catalytic Oxidation of Glutathione and Other Sulfhydryl Compounds by Selenite
Tsen, C. C., & Tappel, A. L. (1958) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77374-8 · Cited by 171
Amino acid sequence of rat kidney gamma-glutamylcysteine synthetase.
Yan, N., & Meister, A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40057-4 · Cited by 170
New coenzyme of methyl transfer, coenzyme M
WOLFE, R. S., & McBride, B. C. (1971) · Biochemistry · doi:10.1021/bi00788a022 · Cited by 170
Component C of the methylreductase system of Methanobacterium.
Ellefson, W. L., & WOLFE, R. S. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69427-5 · Cited by 169
Specificity and biological distribution of coenzyme M (2-mercaptoethanesulfonic acid)
Balch, W. E., & WOLFE, R. S. (1979) · Journal of Bacteriology · doi:10.1128/jb.137.1.256-263.1979 · Cited by 162
Spies, H. S., & Steenkamp, D. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb20013.x · Cited by 153
Enzyme-catalyzed methyl transfers to thiols: the role of zinc
Matthews, R. G., & Goulding, C. W. (1997) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(97)80070-1 · Cited by 137
Ferguson, D. J., Gorlatova, N. V., Grahame, D. A., & Krzycki, J. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910218199 · Cited by 132
May, M. J., Vernoux, T., Sánchez‐Fernández, R., MONTAGU, M. V., & Inzé, D. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.20.12049 · Cited by 129
Bäumer, S., Ide, T., Jacobi, C., Johann, A., Gottschalk, G., & Deppenmeier, U. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000650200 · Cited by 128
Novel biochemical pathways in parasitic protozoa
Fairlamb, A. H. (1989) · Parasitology · doi:10.1017/s003118200008344x · Cited by 128
Newton, G. L., Bewley, C. A., Dwyer, T. J., Horn, R., Aharonowitz, Y., Cohen, G., DAVIES, J. E., Faulkner, D. J., & Fahey, R. C. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.0821h.x · Cited by 122
Self-citationAnaerobic bacterial metabolism in the ancient eukaryote Giardia duodenalis
Brown, D. M., Upcroft, J., Edwards, M. R., & Upcroft, P. (1998) · International Journal for Parasitology · doi:10.1016/s0020-7519(97)00172-0 · Cited by 121
Methanol: Coenzyme M Methyltransferase from Methanosarcina Barkeri
Sauer, K., Harms, U., & Thauer, R. K. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-1-00670.x · Cited by 121
Novel reactions involved in energy conservation by methanogenic archaea
Deppenmeier, U., Lienard, T., & Gottschalk, G. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01026-1 · Cited by 117
delCardayré, S. B., Stock, K. P., Newton, G. L., Fahey, R. C., & DAVIES, J. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.10.5744 · Cited by 116
Self-citationBiosynthesis of Ergothioneine and Hercynine by Fungi and Actinomycetales
Genghof, D. S. (1970) · Journal of Bacteriology · doi:10.1128/jb.103.2.475-478.1970 · Cited by 113
Held, K. D., & Biaglow, J. E. (1994) · Radiation Research · doi:10.2307/3578727 · Cited by 113
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
Melville, D. B. (1959) · Vitamins and hormones · doi:10.1016/s0083-6729(08)60271-x · Cited by 109
Newton, G. L., Av‐Gay, Y., & Fahey, R. C. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.24.6958-6963.2000 · Cited by 106
Self-citationExpression, Purification, and Characterization of Mycobacterium tuberculosis Mycothione Reductase
Patel, M. P., & Blanchard, J. S. (1999) · Biochemistry · doi:10.1021/bi991025h · Cited by 105
WOLFE, R. S. (1991) · Annual Review of Microbiology · doi:10.1146/annurev.mi.45.100191.000245 · Cited by 99
Newton, G. L., Unson, M. D., Anderberg, S. J., Aguilera, J. A., Oh, N. N., delCardayré, S. B., Av‐Gay, Y., & Fahey, R. C. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0156 · Cited by 97
Self-citationImport and Metabolism of Glutathione by Streptococcus mutans
Sherrill, C. B., & Fahey, R. C. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.6.1454-1459.1998 · Cited by 97
Self-citationERGOTHIONEINE IN MICROORGANISMS
Melville, D. B., Genghof, D. S., Inamine, E., & Kovalenko, V. (1956) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65113-0 · Cited by 95
Noll, K. M., Rinehart, K. L., Tanner, R. S., & WOLFE, R. S. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.12.4238 · Cited by 94
BIOSYNTHESIS OF ERGOTHIONEINE AND HERCYNINE BY MYCOBACTERIA
Genghof, D. S., & Damme, O. V. (1964) · Journal of Bacteriology · doi:10.1128/jb.87.4.852-862.1964 · Cited by 90
ASMUS, K.-D., BENSASSON, R. V., BERNIER, J.-L., HOUSSIN, R., & LAND, E. J. (1996) · Biochemical Journal · doi:10.1042/bj3150625 · Cited by 89
Glutathionylspermidine Metabolism in Escherichia coli.
Bollinger, J. M., Jr., Kwon, D. S., Huisman, G. W., Kolter, R., & Walsh, C. T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.23.14031 · Cited by 89
Low-molecular-weight thiols in streptomycetes and their potential role as antioxidants
Newton, G. L., Fahey, R. C., Cohen, G., & Aharonowitz, Y. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.9.2734-2742.1993 · Cited by 88
Self-citationEllis, J. E., Yarlett, N., Cole, D., Humphreys, M. J., & Lloyd, D. (1994) · Microbiology · doi:10.1099/13500872-140-9-2489 · Cited by 88
The Biosynthesis of Methylated Amino Acids in the Active Site Region of Methyl-coenzyme M Reductase
Selmer, T., Kahnt, J., Goubeaud, M., Shima, S., Grabarse, W., Ermler, U., & Thauer, R. K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.6.3755 · Cited by 86
GÄRTNER, P., Ecker, A., Fischer, R., Linder, D., Fuchs, G., & Thauer, R. K. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17792.x · Cited by 86
Zinc-catalyzed sulfur alkylation: insights from protein farnesyltransferase
Hightower, K. E., & Fierke, C. A. (1999) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)80030-1 · Cited by 85
Overview of coenzyme A metabolism and its role in cellular toxicity
Brass, E. P. (1994) · Chemico-Biological Interactions · doi:10.1016/0009-2797(94)90010-8 · Cited by 83
Biosynthesis of mycothiol: elucidation of the sequence of steps in Mycobacterium smegmatis
Bornemann, C., Jardine, A. M., Spies, H. S. C., & Steenkamp, D. J. (1997) · Biochemical Journal · doi:10.1042/bj3250623 · Cited by 82
Weber, A. L. (1998) · Origins of Life and Evolution of Biospheres · doi:10.1023/a:1006524818404 · Cited by 80
Harms, U., Weiss, D. S., Gärtner, P., Linder, D., & Thauer, R. K. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.0640m.x · Cited by 79
Methylcobalamin:Coenzyme M Methyltransferase Isoenzymes MtaA and MtbA from Methanosarcina barkeri
Harms, U., & Thauer, R. K. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.00653.x · Cited by 78
Ide, T., Bäumer, S., & Deppenmeier, U. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.13.4076-4080.1999 · Cited by 77
Prebiotic Synthesis of Methionine
Trump, J. E. V., & Miller, S. L. (1972) · Science · doi:10.1126/science.178.4063.859 · Cited by 77
gamma-Glutamylcysteine and thiosulfate are the major low-molecular-weight thiols in halobacteria
Newton, G. L., & Javor, B. J. (1985) · Journal of Bacteriology · doi:10.1128/jb.161.1.438-441.1985 · Cited by 74
The Function of γ-Glutamylcysteine and Bis-γ-glutamylcystine Reductase in Halobacterium halobium
Sundquist, A. R., & Fahey, R. C. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85002-0 · Cited by 73
Self-citationSynthesis of Cystine in Simulated Primitive Conditions
Khare, B. N., & Sagan, C. (1971) · Nature · doi:10.1038/232577a0 · Cited by 73
Mycothiol Biosynthesis and Metabolism
Anderberg, S. J., Newton, G. L., & Fahey, R. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.46.30391 · Cited by 72
Self-citationBlueprint for a cell: the nature and origin of life
Cairns-Smith, A. G. (1991) · Endeavour · doi:10.1016/0160-9327(91)90128-x · Cited by 72
The evolution of glutathione metabolism in phototrophic microorganisms
Fahey, R. C., Buschbacher, R. M., & Newton, G. L. (1987) · Journal of Molecular Evolution · doi:10.1007/bf02100044 · Cited by 70
Self-citationPeptostreptococcus micros has a uniquely high capacity to form hydrogen sulfide from glutathione
Carlsson, J., Larsen, J. T., & Edlund, M. B. (1993) · Oral Microbiology and Immunology · doi:10.1111/j.1399-302x.1993.tb00541.x · Cited by 67
Sakuda, S., Zhou, Z., & Yamada, Y. (1994) · Bioscience, biotechnology and biochemistry · doi:10.1271/bbb.58.1347 · Cited by 65
Graupner, M., Xu, H., & White, R. H. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.13.3688-3692.2000 · Cited by 64
Graupner, M., Xu, H., & White, R. H. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.17.4862-4867.2000 · Cited by 62
delCardayré, S. B., & DAVIES, J. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.10.5752 · Cited by 61
Misset-Smits, M., OPHEM, P. W. V., Sakuda, S., & Duine, J. A. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00510-3 · Cited by 61
Methyl‐coenzyme M formation in methanogenic archaea
Sauer, K., & Thauer, R. K. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01245.x · Cited by 60
Cysteine is the major low-molecular weight thiol in Giardia duodenalis
Brown, ]. M., Upcroft, J., & Upcroft, P. (1993) · Molecular and Biochemical Parasitology · doi:10.1016/0166-6851(93)90169-x · Cited by 59
Lienard, T., Becher, B., Marschall, M., Bowien, S., & Gottschalk, G. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0857u.x · Cited by 58
THE BIOSYNTHESIS OF ERGOTHIONEINE
Melville, D. B., Eich, S., & Ludwig, M. L. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64979-8 · Cited by 56
Sur une base nouvelle retiree du seigle ergote, l'ergothioneine
Tanret, C. (1909) · Medical Entomology and Zoology · Cited by 54
Gärtner, P., Weiss, D. S., Harms, U., & Thauer, R. K. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb20071.x · Cited by 51
Norin, A., OPHEM, P. W. V., Piersma, S. R., Persson, B., Duine, J. A., & Jörnvall, H. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00282.x · Cited by 50
Biosynthesis of the methanogenic cofactors
White, R. H. (2001) · Vitamins and hormones · doi:10.1016/s0083-6729(01)61010-0 · Cited by 49
Thiol : fumarate reductase (Tfr) from Methanobacterium thermoautotrophicum
Heim, S., Künkel, A., Thauer, R. K., & Hedderich, R. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2530292.x · Cited by 47
Lüersen, K., Walter, R., & Müller, S. (1999) · Molecular and Biochemical Parasitology · doi:10.1016/s0166-6851(98)00161-3 · Cited by 45
White, R. H. (1988) · Biochemistry · doi:10.1021/bi00419a043 · Cited by 42
Estimation of Methanogen Biomass by Quantitation of Coenzyme M
Elias, D. A., Krumholz, L. R., Tanner, R. S., & Suflita, J. M. (1999) · Applied and Environmental Microbiology · doi:10.1128/aem.65.12.5541-5545.1999 · Cited by 42
Future prospects for the chemotherapy of Chagas' disease.
Fairlamb, A. H. (1999) · PubMed · Cited by 41
Fahey, R. C. (1977) · Advances in experimental medicine and biology · doi:10.1007/978-1-4684-3282-4_1 · Cited by 41
Self-citationThe F420H2:heterodisulfide oxidoreductase system from Methanosarcina species
Bäumer, S., Murakami, E., Brodersen, J., Gottschalk, G., Ragsdale, S. W., & Deppenmeier, U. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00555-9 · Cited by 41
Kwon, D. S., Lin, C.-H., Chen, S., Coward, J. K., Walsh, C. T., & Bollinger, J. M., Jr. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.4.2429 · Cited by 41
Glutathione amide and its perthiol in anaerobic sulfur bacteria
Bartsch, R. G., Newton, G. L., Sherrill, C., & Fahey, R. C. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.15.4742-4746.1996 · Cited by 40
Self-citationKrum, J. G., & Ensign, S. A. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.9.2629-2634.2000 · Cited by 39
Intermediates in the biosynthesis of coenzyme M (2-mercaptoethanesulfonic acid)
White, R. H. (1986) · Biochemistry · doi:10.1021/bi00366a047 · Cited by 38
Glutathione Accumulation in Lactococci
Wiederholt, K. M., & Steele, J. L. (1994) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(94)77056-9 · Cited by 38
Noll, K. M., & WOLFE, R. S. (1987) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(87)91307-6 · Cited by 36
Evidence for conjugates between polyamines and glutathione in E. coli
Dubin, D. T. (1959) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(59)90034-8 · Cited by 35
Disulfide reduction and sulfhydryl uptake by Streptococcus mutans
Thomas, E. L. (1984) · Journal of Bacteriology · doi:10.1128/jb.157.1.240-246.1984 · Cited by 35
Sundquist, A. R., & Fahey, R. C. (1988) · Journal of Bacteriology · doi:10.1128/jb.170.8.3459-3467.1988 · Cited by 34
Self-citationBiosynthesis of coenzyme M (2-mercaptoethanesulfonic acid)
White, R. H. (1985) · Biochemistry · doi:10.1021/bi00344a027 · Cited by 33
Clark, D. D., Allen, J. R., & Ensign, S. A. (2000) · Biochemistry · doi:10.1021/bi992282p · Cited by 33
Swerdlow, R. D., & Setlow, P. (1983) · Journal of Bacteriology · doi:10.1128/jb.153.1.475-484.1983 · Cited by 32
Kumaresan, K. R., Springhorn, S. S., & Lacks, S. A. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.13.3641-3646.1995 · Cited by 29
Patel, M. P., & Blanchard, J. S. (1998) · Journal of the American Chemical Society · doi:10.1021/ja983111v · Cited by 28
Bobik, T. A., & WOLFE, R. S. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)51526-x · Cited by 27
Lin, C., Kwon, D. S., Bollinger, J. M., Jr., & Walsh, C. T. (1997) · Biochemistry · doi:10.1021/bi9714464 · Cited by 27
An immunoassay for the detection and quantitative determination of mycothiol
Unson, M. D., Newton, G. L., Davis, C. E. L. B., & Fahey, R. C. (1998) · Journal of Immunological Methods · doi:10.1016/s0022-1759(98)00034-9 · Cited by 26
Self-citationSteps in the conversion of .alpha.-ketosuberate to 7-mercaptoheptanoic acid in methanogenic bacteria
White, R. H. (1989) · Biochemistry · doi:10.1021/bi00450a026 · Cited by 22
Lienard, T., & Gottschalk, G. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00229-4 · Cited by 21
The role of sulphur in chemical evolution
Raulin, F., & Toupance, G. (1977) · Journal of Molecular Evolution · doi:10.1007/bf01796095 · Cited by 19
Improved Methods for Immunoassay of Mycothiol
Unson, M. D., Newton, G. L., Arnold, K. F., Davis, C. E. L. B., & Fahey, R. C. (1999) · Journal of Clinical Microbiology · doi:10.1128/jcm.37.7.2153-2157.1999 · Cited by 12
Self-citationBiosynthesis of (7-Mercaptoheptanoyl)threonine phosphate
White, R. H. (1994) · Biochemistry · doi:10.1021/bi00189a009 · Cited by 11
Biosynthesis of the Peptide Bond in the CoenzymeN-(7-Mercaptoheptanoyl)-l-threonine Phosphate
Solow, B. T., & White, R. H. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0272 · Cited by 11
Glutathionylspermidine in Escherichia coli.
Tabor, H., & Cw, T. (1976) · PubMed · Cited by 10
Harms, U., Weiss, D. S., Gartner, P., et al. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20303.x · Cited by 9
Newton, G. L., Bewley, C. A., Dwyer, T. J., et al. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20626.x · Cited by 6
Vergauwen, B., Guisez, Y., Bartsch, R. G., Meyer, T., Cusanovich, M., & BEEUMEN, J. V. (1999) · Ghent University Academic Bibliography (Ghent University) · Cited by 1
Flagged first, then by citations
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
Cited by
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
Metadata
- 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
- 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