{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T21:31:56Z","timestamp":1792272716541,"version":"4.4.0"},"reference-count":83,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2020,3,12]],"date-time":"2020-03-12T00:00:00Z","timestamp":1583971200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>Sulfate is present in foods, beverages, and drinking water. Its reduction and concentration in the gut depend on the intestinal microbiome activity, especially sulfate-reducing bacteria (SRB), which can be involved in inflammatory bowel disease (IBD). Assimilatory sulfate reduction (ASR) is present in all living organisms. In this process, sulfate is reduced to hydrogen sulfide and then included in cysteine and methionine biosynthesis. In contrast to assimilatory sulfate reduction, the dissimilatory process is typical for SRB. A terminal product of this metabolism pathway is hydrogen sulfide, which can be involved in gut inflammation and also causes problems in industries (due to corrosion effects). The aim of the review was to compare assimilatory and dissimilatory sulfate reduction (DSR). These processes occur in some species of intestinal bacteria (e.g., Escherichia and Desulfovibrio genera). The main attention was focused on the description of genes and their location in selected strains. Their coding expression of the enzymes is associated with anabolic processes in various intestinal bacteria. These analyzed recent advances can be important factors for proposing possibilities of metabolic pathway extension from hydrogen sulfide to cysteine in intestinal SRB. The switch from the DSR metabolic pathway to the ASR metabolic pathway is important since toxic sulfide is not produced as a final product.<\/jats:p>","DOI":"10.3390\/cells9030698","type":"journal-article","created":{"date-parts":[[2020,3,13]],"date-time":"2020-03-13T08:58:59Z","timestamp":1584089939000},"page":"698","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":219,"title":["Recent Advances in Metabolic Pathways of Sulfate Reduction in Intestinal Bacteria"],"prefix":"10.3390","volume":"9","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8450-7137","authenticated-orcid":false,"given":"Ivan","family":"Kushkevych","sequence":"first","affiliation":[{"name":"Department of Experimental Biology, Faculty of Science, Masaryk University, Kamenice 753\/5, 62500 Brno, Czech Republic"},{"name":"Department of Molecular Biology and Pharmaceutical Biotechnology, University of Veterinary and Pharmaceutical Sciences Brno, 61242 Brno, Czech Republic"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9340-9793","authenticated-orcid":false,"given":"Ji\u0159\u00ed","family":"Cejnar","sequence":"additional","affiliation":[{"name":"Department of Experimental Biology, Faculty of Science, Masaryk University, Kamenice 753\/5, 62500 Brno, Czech Republic"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jakub","family":"Treml","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology and Pharmaceutical Biotechnology, University of Veterinary and Pharmaceutical Sciences Brno, 61242 Brno, Czech Republic"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2435-9726","authenticated-orcid":false,"given":"Dani","family":"Dordevi\u0107","sequence":"additional","affiliation":[{"name":"Department of Plant Origin Foodstuffs Hygiene and Technology, Faculty of Veterinary Hygiene and Ecology, University of Veterinary and Pharmaceutical Sciences, 61242 Brno, Czech Republic"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter","family":"Kollar","sequence":"additional","affiliation":[{"name":"Department of Human Pharmacology and Toxicology, Faculty of Pharmacy, University of Veterinary and Pharmaceutical Sciences, 61242 Brno, Czech Republic"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Monika","family":"V\u00edt\u011bzov\u00e1","sequence":"additional","affiliation":[{"name":"Department of Experimental Biology, Faculty of Science, Masaryk University, Kamenice 753\/5, 62500 Brno, Czech Republic"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,3,12]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/S0065-2164(09)01202-7","article-title":"Biochemistry, physiology and biotechnology of sulfate-reducing bacteria","volume":"68","author":"Barton","year":"2009","journal-title":"Adv. Appl. Microbiol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"448","DOI":"10.3389\/fphys.2012.00448","article-title":"Microbial pathways in colonic sulfur metabolism and links with health and disease","volume":"3","author":"Carbonero","year":"2012","journal-title":"Front. Physiol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1716","DOI":"10.1136\/gutjnl-2018-316723","article-title":"Human gut microbiome: Hopes, threats and promises","volume":"67","author":"Cani","year":"2018","journal-title":"Gut"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"197","DOI":"10.30970\/sbi.1001.560","article-title":"Dissimilatory sulfate reduction in the intestinal sulfate-reducing bacteria","volume":"10","author":"Kushkevych","year":"2016","journal-title":"Studia Biologica"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1007\/s00203-019-01625-z","article-title":"Toxicity of hydrogen sulfide toward sulfate-reducing bacteria Desulfovibrio piger Vib-7","volume":"201","author":"Kushkevych","year":"2019","journal-title":"Arch. Microbiol."},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Kushkevych, I., Dordevi\u0107, D., Kollar, P., V\u00edt\u011bzov\u00e1, M., and Drago, L. (2019). Hydrogen Sulfide as a Toxic Product in the Small\u2013Large Intestine Axis and its Role in IBD Development. J. Clin. Med., 8.","DOI":"10.3390\/jcm8071054"},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Kushkevych, I., Kotrsov\u00e1, V., Dordevi\u0107, D., Bu\u0148kov\u00e1, L., V\u00edt\u011bzov\u00e1, M., and Amedei, A. (2019). Hydrogen Sulfide Effects on the Survival of Lactobacilli with Emphasis on the Development of Inflammatory Bowel Diseases. Biomolecules, 9.","DOI":"10.3390\/biom9120752"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"4066","DOI":"10.33263\/BRIAC94.066069","article-title":"Possible methods for evaluation of hydrogen sulfide toxicity against lactic acid bacteria","volume":"9","author":"Kushkevych","year":"2019","journal-title":"Biointerface Res. Appl. Chem."},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Kushkevych, I., Le\u0161\u010danov\u00e1, O., Dordevi\u0107, D., Jan\u010d\u00edkov\u00e1, S., Ho\u0161ek, J., V\u00edt\u011bzov\u00e1, M., Bu\u0148kov\u00e1, L., and Drago, L. (2019). The Sulfate-Reducing Microbial Communities and Meta-Analysis of Their Occurrence during Diseases of Small\u2013Large Intestine Axis. J. Clin. Med., 8.","DOI":"10.3390\/jcm8101656"},{"key":"ref_10","first-page":"237","article-title":"Hydrogen sulfide: A toxic gas produced by dissimilatory sulfate and sulfur reduction and consumed by microbial oxidation","volume":"14","author":"Barton","year":"2014","journal-title":"Met. Ions Life Sci."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1111\/j.1574-6941.1993.tb00023.x","article-title":"Metabolic interactions involving sulfate-reducing and methanogenic bacteria in the human large intestine","volume":"12","author":"Gibson","year":"1993","journal-title":"FEMS Microbiol. Ecol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1111\/j.1365-2672.1988.tb01498.x","article-title":"Occurrence of sulfate-reducing bacteria in human faeces and the relationship of dissimilatory sulfate reduction to methanogenesis in the large gut","volume":"65","author":"Gibson","year":"1988","journal-title":"J. Appl. Bacteriol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1111\/j.1365-2672.1990.tb01575.x","article-title":"Physiology and ecology of the sulfate-reducing bacteria","volume":"69","author":"Gibson","year":"1990","journal-title":"J. Appl. Bacteriol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"3","DOI":"10.2754\/avb201585010003","article-title":"Activity of Na+\/K+-activated Mg2+-dependent ATP hydrolase in the cell-free extracts of the sulfate-reducing bacteria Desulfovibrio piger Vib-7 and Desulfomicrobium sp. Rod-9","volume":"84","author":"Kushkevych","year":"2015","journal-title":"Acta Vet. Brno."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"107","DOI":"10.33073\/pjm-2015-016","article-title":"Kinetic Properties of Pyruvate Ferredoxin Oxidoreductase of Intestinal Sulfate-Reducing Bacteria Desulfovibrio piger Vib-7 and Desulfomicrobium sp. Rod-9","volume":"64","author":"Kushkevych","year":"2015","journal-title":"Pol. J. Microbiol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/j.jab.2018.01.004","article-title":"Effect of selected 8-hydroxyquinoline- 2-carboxanilides on viability and sulfate metabolism of Desulfovibrio piger","volume":"16","author":"Kushkevych","year":"2018","journal-title":"J. Appl. Biomed."},{"key":"ref_17","first-page":"106","article-title":"Activity of selected salicylamides against intestinal sulfate-reducing bacteria","volume":"36","author":"Kushkevych","year":"2015","journal-title":"Neuro Endocrinol. Lett."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"2975","DOI":"10.1128\/JB.180.11.2975-2982.1998","article-title":"Phylogeny of dissimilatory sulfite reductases supports an early origin of sulfate respiration","volume":"180","author":"Wagner","year":"1998","journal-title":"J. Bacteriol."},{"key":"ref_19","first-page":"1037","article-title":"Activity and kinetic properties of phosphotransacetylase from intestinal sulfate-reducing bacteria","volume":"62","author":"Kushkevych","year":"2015","journal-title":"Acta Biochem. Pol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.2478\/s11756-018-0118-2","article-title":"Cross-correlation analysis of the Desulfovibrio growth parameters of intestinal species isolated from people with colitis","volume":"73","author":"Kushkevych","year":"2018","journal-title":"Biologia"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1515\/med-2019-0010","article-title":"Analysis of pH dose-dependent growth of sulfate-reducing bacteria","volume":"14","author":"Kushkevych","year":"2019","journal-title":"Open Med. (Wars.)"},{"key":"ref_22","first-page":"49","article-title":"Pathways of assimilatory sulphate reduction in plants and microorganisms","volume":"72","author":"Schiff","year":"1979","journal-title":"Ciba Found. Symp."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1006\/jfca.1993.1016","article-title":"The sulfate content of foods and beverages","volume":"6","author":"Florin","year":"1993","journal-title":"J. Food Compos. Anal."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"16568","DOI":"10.1016\/S0021-9258(18)37428-3","article-title":"In vivo studies of cysteine metabolism. Use of D-cysteinesulfinate, a novel cysteinesulfinate decarboxylase inhibitor, to probe taurine and pyruvate synthesis","volume":"263","author":"Weinstein","year":"1988","journal-title":"J. Biol. Chem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1515\/med-2018-0052","article-title":"Metabolic activity of sulfate-reducing bacteria from rodents with colitis","volume":"13","author":"Kushkevych","year":"2018","journal-title":"Open Med. (Wars.)"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"405","DOI":"10.2754\/avb201786040405","article-title":"Kinetic properties of growth of intestinal sulphate-reducing bacteria isolated from healthy mice and mice with ulcerative colitis","volume":"86","author":"Kushkevych","year":"2017","journal-title":"Acta Vet. Brno"},{"key":"ref_27","first-page":"3405","article-title":"Bilophila wadsworthia, gen-nov and sp-nov, a unique Gram-negative Anaerobic rod recovered from appendicitis specimens and human feces","volume":"135","author":"Baron","year":"1989","journal-title":"J. Gen. Microbiol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1099\/mic.0.27573-0","article-title":"A sulfite respiration system in the chemoheterotrophic human pathogen Campylobacter jejuni","volume":"151","author":"Kelly","year":"2005","journal-title":"Microbiology"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1128\/jb.70.6.735-737.1955","article-title":"The L-cysteine desulfhydrase of Escherichia coli","volume":"70","author":"Metaxas","year":"1955","journal-title":"J. Bacteriol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"986","DOI":"10.1126\/science.1209855","article-title":"H2S: A universal defense against antibiotics in bacteria","volume":"334","author":"Shatalin","year":"2011","journal-title":"Science"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"7157","DOI":"10.1016\/S0021-9258(19)44608-5","article-title":"Purification and subunits structure of cysteine desulfhydrase from Salmonella typhimurium","volume":"247","author":"Kredich","year":"1972","journal-title":"J. Biol. Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"8069","DOI":"10.1074\/jbc.M412540200","article-title":"Functional demonstration of reverse transsulfuration in the Mycobacterium tuberculosis complex reveals that methionine is the preferred sulfur source for pathogenic mycobacteria","volume":"280","author":"Wheeler","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1097\/00004836-200605000-00011","article-title":"Volatile sulfur compounds produced by Helicobacter pylori","volume":"40","author":"Kim","year":"2006","journal-title":"J. Clin. Gastroenterol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1111\/j.1399-302X.2009.00546.x","article-title":"Characterization of L-cysteine desulfhydrase from Prevotella intermedia","volume":"24","author":"Yano","year":"2009","journal-title":"Oral Microbiol. Immunol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"2260","DOI":"10.1099\/mic.0.039180-0","article-title":"Production of hydrogen sulfide by two enzymes associated with biosynthesis of homocysteine and lanthionine in Fusobacterium nucleatum subsp. pnucleatum ATCC25586","volume":"156","author":"Yoshida","year":"2010","journal-title":"Microbiology"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1111\/j.2041-1014.2010.00599.x","article-title":"Streptococcus anginosusl cysteine desulfhydrase gene expression is associated with abscess formationin BALB\/c mice","volume":"26","author":"Yoshida","year":"2011","journal-title":"Mol. Oral Microbiol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1111\/j.1574-6968.2000.tb09265.x","article-title":"Prevotella enzymes involved in mucin oligosaccharide degradation and evidence for a small operon of genes expressed during growth on mucin","volume":"190","author":"Wright","year":"2000","journal-title":"FEMS Microbiol. Lett."},{"key":"ref_38","first-page":"1132","article-title":"Glycosulfatase activity of Helicobacter pylori toward human gastric mucin effect of sucralfate","volume":"87","author":"Slomiany","year":"1992","journal-title":"Am. J. Gastroenterol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1515\/biol-2017-0009","article-title":"Production of biogas: Relationship between methanogenic and sulfate-reducing microorganisms","volume":"12","author":"Kushkevych","year":"2017","journal-title":"Open Life Sci."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1515\/biol-2018-0017","article-title":"A new combination of substrates: Biogas production and diversity of the methanogenic microorganisms","volume":"13","author":"Kushkevych","year":"2018","journal-title":"Open Life Sci."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1515\/biol-2018-0057","article-title":"Analysis of physiological parameters of Desulfovibrio strains from individuals with colitis","volume":"13","author":"Kushkevych","year":"2018","journal-title":"Open Life Sci."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1128\/JB.184.1.278-289.2002","article-title":"Phylogenetic analysis reveals multiple lateral transfers of adenosine-5\u2019-phosphosulfate reductase genes among sulfate-reducing microorganisms","volume":"184","author":"Friedrich","year":"2002","journal-title":"J. Bacteriol."},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Dworkin, M., Falkow, S., Rosenberg, E., Schleifer, K.H., and Stackenbrandt, E. (2006). Dissimilatory Sulfate and Sulfur-Reducing Prokaryotes. The Prokaryotes, Springer.","DOI":"10.1007\/0-387-30745-1"},{"key":"ref_44","unstructured":"Barton, L.L., and Hamilton, W.A. (2010). Sulfate-Reducing Bacteria: Environmental and Engineered Systems, Cambridge University Press."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/0006-291X(70)90579-6","article-title":"A flavin-sulfite adduct as an intermediate in the reaction catalyzed by adenylyl sulfate reductase from Desulfovibrio vulgaris","volume":"39","author":"Michaels","year":"1970","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"554","DOI":"10.1038\/nbt959","article-title":"The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough","volume":"22","author":"Heidelberg","year":"2004","journal-title":"Nat. Biotechnol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"1541","DOI":"10.1126\/science.aad3558","article-title":"A protein trisulfide couples dissimilatory sulfate reduction to energy conservation","volume":"350","author":"Santos","year":"2015","journal-title":"Science"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"34141","DOI":"10.1074\/jbc.M805643200","article-title":"The crystal structure of Desulfovibrio vulgaris dissimilatory sulfite reductase bound to DsrC provides novel insights into the mechanism of sulfate respiration","volume":"283","author":"Oliveira","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_49","first-page":"112","article-title":"Purification and characteriztion of bisulfite reductase (desulfofuscidin) from Desulfovibrio thermophilus and its complexes with exogenous ligands","volume":"1040","author":"Fauque","year":"1990","journal-title":"Biochem. Biophys. Acta"},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Kushkevych, I., Cejnar, J., V\u00edt\u011bzov\u00e1, M., V\u00edt\u011bz, T., Dordevi\u0107, D., and Bomble, Y.J. (2020). Occurrence of Thermophilic Microorganisms in Different Full Scale Biogas Plants. Int. J. Mol. Sci, 21.","DOI":"10.3390\/ijms21010283"},{"key":"ref_51","unstructured":"Shively, J.M., and Barton, L.L. (1991). Sulfur reductase from thiophilic sulfate-reducing bacteria. Variations in Autotrophic Life, Academic Press."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1128\/aem.61.1.290-296.1995","article-title":"Conservation of the Genes for Dissimilatory Sulfite Reductase from Desulfovibrio vulgaris and Archaeoglobus fulgidus Allows Their Detection by PCR","volume":"61","author":"Huber","year":"1995","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1007\/s00203-018-1510-6","article-title":"The diversity of sulfate-reducing bacteria in the seven bioreactors","volume":"200","author":"Kushkevych","year":"2018","journal-title":"Arch. Microbiol."},{"key":"ref_54","unstructured":"Kov\u00e1\u010d, J., and Kushkevych, I. (2019, January 6\u20137). New modification of cultivation medium for isolation and growth of intestinal sulfate-reducing bacteria. Proceedings of the International PhD Students Conference Mendel Net, Brno, Czech Republic."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.jab.2016.01.005","article-title":"Antimicrobial effect of salicylamide derivatives against intestinal sulfate-reducing bacteria","volume":"14","author":"Kushkevych","year":"2016","journal-title":"J. Appl. Biomed."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1097\/00004836-200603000-00015","article-title":"Colonic health: Fermentation and short chain fatty acids","volume":"40","author":"Wong","year":"2006","journal-title":"J. Clin. Gastroenterol."},{"key":"ref_57","unstructured":"Zehnder, A.J.B. (1988). Biology of Anaerobic Microorganisms, John Wiley and Sons."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1007\/s10482-009-9383-y","article-title":"Effect of sulfide on growth physiology and gene expression of Desulfovibrio vulgaris Hildenborough","volume":"97","author":"Caffrey","year":"2010","journal-title":"Antonie Van Leeuwenhoek"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1002\/bjs.6454","article-title":"Sulphate-reducing bacteria and hydrogen sulphide in the etiology of ulcerative colitis","volume":"96","author":"Rowan","year":"2009","journal-title":"Br. J. Surg."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1152\/physrev.00017.2011","article-title":"Psysiological implications of hydrogen sulfide: A whiff exploration that blossomed","volume":"92","author":"Wang","year":"2012","journal-title":"Physiol. Rev."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1016\/S0140-6736(80)91934-0","article-title":"The colonic epithelium in ulcerative colitis: An energy-deficiency disease?","volume":"2","author":"Roediger","year":"1980","journal-title":"Lancet"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"6409","DOI":"10.1021\/ja01605a029","article-title":"The enzymatic sequence in the biosynthesis of active sulfate","volume":"78","author":"Robbins","year":"1956","journal-title":"J. Am. Chem. Soc."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1587","DOI":"10.1016\/S0021-9258(19)42922-0","article-title":"Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. IV. The Escherichia coli hemoflavoprotein subunit structure and dissociation into hemoprotein and flavoprotein components","volume":"249","author":"Siegel","year":"1974","journal-title":"J. Biol. Chem."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1128\/ecosalplus.3.6.1.11","article-title":"Biosynthesis of Cystein","volume":"3","author":"Kredich","year":"2008","journal-title":"EcoSal Plus"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"2428","DOI":"10.1016\/S0021-9258(19)78241-6","article-title":"Purification and characterization of cysteine synthetase, a bifunctional protein complex, from Salmonella typhimurium","volume":"244","author":"Kredich","year":"1969","journal-title":"J. Biol. Chem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1093\/nar\/gkj405","article-title":"Escherichia coli K-12: A cooperatively developer annotation snapshot","volume":"34","author":"Riley","year":"2006","journal-title":"Nucleic Acids Res."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"3351","DOI":"10.1128\/jb.172.6.3351-3357.1990","article-title":"Sulfate and thiosulfate transport in Escherichia coli K-12: Nucleotide sequence and expression of the cysTWAM gene cluster","volume":"172","author":"Sirko","year":"1990","journal-title":"J. Bacteriol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"15012","DOI":"10.1016\/S0021-9258(18)63804-9","article-title":"Adenosine-5-phosphosulfate kinase from Escherichia coli KI2","volume":"264","author":"Satishchandran","year":"1989","journal-title":"J. Biol. Chem."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1146\/annurev.bi.52.070183.001155","article-title":"Biochemistry of sulfur-containing amino acids","volume":"52","author":"Cooper","year":"1983","journal-title":"Annu. Rev. Biochem."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1007\/BF00269864","article-title":"Characterisation of the gene cysH and of its product phospho-adenylylsulfate reductase from Escherichia coli","volume":"225","author":"Krone","year":"1991","journal-title":"Mol. Gen. Genet."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"37651","DOI":"10.1074\/jbc.M005619200","article-title":"A simplified functional version of the Escherichia coli sulfite reductase","volume":"275","author":"Zeghouf","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1128\/jb.173.1.325-333.1991","article-title":"High-level expression of Escherichia coli NADPH-sulfite reductase: Requirement for a cloned cysG plasmid to overcome limiting siroheme cofactor","volume":"173","author":"Wu","year":"1991","journal-title":"J. Bacteriol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1074\/jbc.275.1.461","article-title":"Serine acetyltransferase from Escherichia coli is a dimer of trimers","volume":"275","author":"Hindson","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1128\/jb.140.1.141-146.1979","article-title":"Regulation of O-acetylserine sulfhydrylase B by L-cysteine in Salmonella typhimurium","volume":"140","author":"Hulanicka","year":"1979","journal-title":"J. Bacteriol."},{"key":"ref_75","unstructured":"Whitford, D. (2005). Proteins: Structure and Function, Wiley."},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Barnes, M.R. (2007). Bioinformatics for Geneticists: A Bioinformatics Primer for the Analysis of Genetic Data, Wiley.","DOI":"10.1002\/9780470059180"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1016\/j.tplants.2005.08.006","article-title":"Sulfur metabolism: A versatile platform for launching defence operations","volume":"10","author":"Rausch","year":"2005","journal-title":"Trends. Plant Sci."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1046\/j.1432-1327.1998.2550235.x","article-title":"Interactions between serine acetyltransferase and O-acetylserine(thiol) lyase in higher plants. Structural and kinetic properties of the free and bound enzymes","volume":"255","author":"Droux","year":"1998","journal-title":"Eur. J. Biochem."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1007\/s00044-017-2067-7","article-title":"Activity of ring-substituted 8-hydroxyquinoline- 2-carboxanilides against intestinal sulfate-reducing bacteria Desulfovibrio piger","volume":"27","author":"Kushkevych","year":"2018","journal-title":"Med. Chem. Res."},{"key":"ref_80","doi-asserted-by":"crossref","unstructured":"\u010cern\u00fd, M., V\u00edt\u011bzov\u00e1, M., V\u00edt\u011bz, T., Barto\u0161, M., and Kushkevych, I. (2018). Variation in the Distribution of Hydrogen Producers from the Clostridiales Order in Biogas Reactors Depending on Different Input Substrates. Energies, 11.","DOI":"10.3390\/en11123270"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1128\/jb.82.6.933-939.1961","article-title":"Enzymatic basis for assimilatory and dissimilatory sulfate reduction","volume":"82","author":"Peck","year":"1961","journal-title":"J. Bacteriol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1111\/j.1574-6968.1991.tb04799.x","article-title":"Growth and activities of sulfate-reducing bacteria in gut contents from healthy subjects and patients with ulcerative colitis","volume":"86","author":"Gibson","year":"1991","journal-title":"FEMS Microbiol. Ecol."},{"key":"ref_83","first-page":"673","article-title":"Location on the Escherichia coli genome of a gene specifying O-acetylserine(thiol)lyase","volume":"130","author":"Boronat","year":"1984","journal-title":"J. Gen. Microbiol."}],"container-title":["Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4409\/9\/3\/698\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T09:06:30Z","timestamp":1760173590000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4409\/9\/3\/698"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,3,12]]},"references-count":83,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2020,3]]}},"alternative-id":["cells9030698"],"URL":"https:\/\/doi.org\/10.3390\/cells9030698","relation":{},"ISSN":["2073-4409"],"issn-type":[{"value":"2073-4409","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,3,12]]}}}