Mechanism for the interaction of thiols with methylcobalamin
The reaction between methylcobalamin and ethane-thiol sulfonic acid (Coenzyme M) has been studied under aerobic conditions. For this reaction evidence is presented for a catalytic cycle which promotes homolytic cleavage of the Cobalt-carbon σ-bond to give Cob(II)alamin (B12-r) and methylcoenzyme M a...
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| Published in | Biochimica et biophysica acta Vol. 428; no. 3; pp. 808 - 817 |
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| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
28.05.1976
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| Subjects | |
| Online Access | Get full text |
| ISSN | 0304-4165 0006-3002 1872-8006 |
| DOI | 10.1016/0304-4165(76)90212-9 |
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| Abstract | The reaction between methylcobalamin and ethane-thiol sulfonic acid (Coenzyme M) has been studied under aerobic conditions. For this reaction evidence is presented for a catalytic cycle which promotes homolytic cleavage of the Cobalt-carbon σ-bond to give Cob(II)alamin (B12-r) and methylcoenzyme M as the products. This reaction is especially pertinent to our understanding of the mechanism of methane-biosynthesis.
In addition, we have used 220 MHz
1H NMR and
13C NMR to show that thiols do not react with methylcorrinoids by displacing the base trans-axial to the cobalt-carbon bond. This NMR study is especially important since the coordination of thiols to cobalt has previously been reported to occur by a number of of researh groups including our own. |
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| AbstractList | The reaction between methylcobalamin and ethane-thiol sulfonic acid (Co-enzyme M) has been studied under aerobic conditions. For this reaction evidence is presented for a catalytic cycle which promotes homolytic cleavage of the Cobalt-carbon sigma-bond to give Cob(II)alamin (B12-r) and methylcoenzyme M as the products. This reaction is especially pertinent to our understanding of the mechanism of methane-biosynthesis. In addition, we have used 220 MHZ 1H NMR and 13C NMR to show that thiols do not react with methylcorrinoids by displacing the base trans-axial to the cobalt-carbon bond. This NMR study is especially important since the co-ordination of thiols to cobalt has previously been reported to occur by a number of research groups including our own.The reaction between methylcobalamin and ethane-thiol sulfonic acid (Co-enzyme M) has been studied under aerobic conditions. For this reaction evidence is presented for a catalytic cycle which promotes homolytic cleavage of the Cobalt-carbon sigma-bond to give Cob(II)alamin (B12-r) and methylcoenzyme M as the products. This reaction is especially pertinent to our understanding of the mechanism of methane-biosynthesis. In addition, we have used 220 MHZ 1H NMR and 13C NMR to show that thiols do not react with methylcorrinoids by displacing the base trans-axial to the cobalt-carbon bond. This NMR study is especially important since the co-ordination of thiols to cobalt has previously been reported to occur by a number of research groups including our own. The reaction between methylcobalamin and ethane-thiol sulfonic acid (Co-enzyme M) has been studied under aerobic conditions. For this reaction evidence is presented for a catalytic cycle which promotes homolytic cleavage of the Cobalt-carbon sigma-bond to give Cob(II)alamin (B12-r) and methylcoenzyme M as the products. This reaction is especially pertinent to our understanding of the mechanism of methane-biosynthesis. In addition, we have used 220 MHZ 1H NMR and 13C NMR to show that thiols do not react with methylcorrinoids by displacing the base trans-axial to the cobalt-carbon bond. This NMR study is especially important since the co-ordination of thiols to cobalt has previously been reported to occur by a number of research groups including our own. The reaction between methylcobalamin and ethane-thiol sulfonic acid (Coenzyme M) has been studied under aerobic conditions. For this reaction evidence is presented for a catalytic cycle which promotes homolytic cleavage of the Cobalt-carbon σ-bond to give Cob(II)alamin (B12-r) and methylcoenzyme M as the products. This reaction is especially pertinent to our understanding of the mechanism of methane-biosynthesis. In addition, we have used 220 MHz 1H NMR and 13C NMR to show that thiols do not react with methylcorrinoids by displacing the base trans-axial to the cobalt-carbon bond. This NMR study is especially important since the coordination of thiols to cobalt has previously been reported to occur by a number of of researh groups including our own. |
| Author | Francia, Marie D. Frick, T. Wood, J.M. |
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| References | Schrauzer (BIB6) 1968; 1 McBride, Wolfe (BIB3) 1971; 10 Law, Brown, Lein, Babior, Wood (BIB13) 1971; 10 Taylor, Wolfe (BIB4) 1974; 249 Taylor, Wolfe (BIB5) 1974; 249 Law, Wood (BIB11) 1973; 95 Penley, Brown, Wood (BIB12) 1970; 9 Agnes, Hill, Pratt, Ridsdale, Kennedy, Williams (BIB10) 1971; 252 Schram, Lemaire, Karlson (BIB14) 1955; 77 Wood, Brown (BIB1) 1972; 11 Rudiger (BIB8) 1971; 21 Needham, Matwiyoff, Walker, Hogenkamp (BIB15) 1973; 95 Rudiger, Jaenicke (BIB9) 1973; 1 Taylor, Hanna (BIB7) 1970; 38 Schrauzer, Seck, Holland, Beckham, Rubin, Sibert (BIB16) 1973; 2 Stadtman (BIB2) 1971; 171 Schrauzer (BIB17) 1974; 31 |
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| Snippet | The reaction between methylcobalamin and ethane-thiol sulfonic acid (Coenzyme M) has been studied under aerobic conditions. For this reaction evidence is... The reaction between methylcobalamin and ethane-thiol sulfonic acid (Co-enzyme M) has been studied under aerobic conditions. For this reaction evidence is... |
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| StartPage | 808 |
| SubjectTerms | Binding Sites Disulfides Glutathione Magnetic Resonance Spectroscopy Molecular Conformation Spectrophotometry Sulfhydryl Compounds Vitamin B 12 |
| Title | Mechanism for the interaction of thiols with methylcobalamin |
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