Coenzyme B induced coordination of coenzyme M via its thiol group to Ni(I) of F430 in active methyl-coenzyme M reductase.
Methyl-coenzyme M reductase (MCR) catalyzes the reaction of methyl-coenzyme M (CH3-S-CoM) with coenzyme B (HS-CoB) to methane and CoM-S-S-CoB. At the active site, it contains the nickel porphinoid F430, which has to be in the Ni(I) oxidation state for the enzyme to be active. How the substrates inte...
المؤلفون الرئيسيون: | Finazzo, C, Harmer, J, Bauer, C, Jaun, B, Duin, E, Mahlert, F, Goenrich, M, Thauer, R, Van Doorslaer, S, Schweiger, A |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
2003
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مواد مشابهة
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Coordination and binding geometry of methyl-coenzyme M in the red1m state of methyl-coenzyme M reductase.
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Binding of coenzyme B induces a major conformational change in the active site of methyl-coenzyme M reductase.
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منشور في: (2010)