{"title":"甲烷生物合成中的辅酶M和甲基钴胺素:模型研究的结果","authors":"G.N. Schrauzer, J.H. Grate , R.Nathan Katz","doi":"10.1016/S0006-3061(00)80000-9","DOIUrl":null,"url":null,"abstract":"<div><p>Coenzyme M (2-mercaptoethanesulfonate, HSCH<sub>2</sub>CH<sub>2</sub>SO<sub>3</sub><sup>—</sup>) reacts with methylcobalamin nonenzymatically in the pH-range between 6 and 14 to yield the S-methyl derivative (CH<sub>3</sub>SCH<sub>2</sub>CH<sub>2</sub>SO<sub>3</sub><sup>—</sup>). In addition, and also at lower pH, methane is produced by reductive cleavage of the CoC bond. With methylcobaloximes as the methyl group donors, methane production predominates, with insignificant S-methylation. The initial rates of methane production from methylcobaloximes with coenzyme M as the reductant correlate with the rates of methane production from these substrates with active cell extracts of <em>Methanobacterium M.o.H.</em></p></div>","PeriodicalId":9177,"journal":{"name":"Bioinorganic chemistry","volume":"8 1","pages":"Pages 1-10"},"PeriodicalIF":0.0000,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0006-3061(00)80000-9","citationCount":"7","resultStr":"{\"title\":\"Coenzyme M and methylcobalamin in methane biosynthesis: Results of model studies\",\"authors\":\"G.N. Schrauzer, J.H. Grate , R.Nathan Katz\",\"doi\":\"10.1016/S0006-3061(00)80000-9\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Coenzyme M (2-mercaptoethanesulfonate, HSCH<sub>2</sub>CH<sub>2</sub>SO<sub>3</sub><sup>—</sup>) reacts with methylcobalamin nonenzymatically in the pH-range between 6 and 14 to yield the S-methyl derivative (CH<sub>3</sub>SCH<sub>2</sub>CH<sub>2</sub>SO<sub>3</sub><sup>—</sup>). In addition, and also at lower pH, methane is produced by reductive cleavage of the CoC bond. With methylcobaloximes as the methyl group donors, methane production predominates, with insignificant S-methylation. The initial rates of methane production from methylcobaloximes with coenzyme M as the reductant correlate with the rates of methane production from these substrates with active cell extracts of <em>Methanobacterium M.o.H.</em></p></div>\",\"PeriodicalId\":9177,\"journal\":{\"name\":\"Bioinorganic chemistry\",\"volume\":\"8 1\",\"pages\":\"Pages 1-10\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1978-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S0006-3061(00)80000-9\",\"citationCount\":\"7\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Bioinorganic chemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0006306100800009\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bioinorganic chemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0006306100800009","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Coenzyme M and methylcobalamin in methane biosynthesis: Results of model studies
Coenzyme M (2-mercaptoethanesulfonate, HSCH2CH2SO3—) reacts with methylcobalamin nonenzymatically in the pH-range between 6 and 14 to yield the S-methyl derivative (CH3SCH2CH2SO3—). In addition, and also at lower pH, methane is produced by reductive cleavage of the CoC bond. With methylcobaloximes as the methyl group donors, methane production predominates, with insignificant S-methylation. The initial rates of methane production from methylcobaloximes with coenzyme M as the reductant correlate with the rates of methane production from these substrates with active cell extracts of Methanobacterium M.o.H.