On the assignment of nickel oxidation states of the Ox1,Ox2 forms of methyl-coenzyme M reductase
Journal Article
·
· Journal of the American Chemical Society
Methyl-coenzyme M reductase (MCR) catalyzes the chemical step of methane formation by methanogenic organisms. The reaction involves the two-electron reduction of CH{sub 3}S-CoM by N-7-mercaptoheptanoylthreoinine phosphate (CoB-SH). The authors have employed 35 GHz EPR and ENDOR spectroscopy to resolve the oxidation state of Ni in ox1, ox2 and red1 forms of MCR, isolated from methanobacterium thermoautotrophicum strain Marburg and prepared as described previously.
- Research Organization:
- Northwestern Univ., Evanston, IL (US)
- Sponsoring Organization:
- USDOE; National Science Foundation (NSF); National Institutes of Health (NIH)
- DOE Contract Number:
- FG02-91ER20053
- OSTI ID:
- 20017346
- Journal Information:
- Journal of the American Chemical Society, Vol. 122, Issue 1; Other Information: PBD: 12 Jan 2000; ISSN 0002-7863
- Country of Publication:
- United States
- Language:
- English
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