In vivo activation of methyl-coenzyme M reductase by carbon monoxide

Zhou, Yuzhen; Dorchak, Alexandria E.; Ragsdale, Stephen W.

doi:10.3389/fmicb.2013.00069

In vivo activation of methyl-coenzyme M reductase by carbon monoxide

Journal Article · Tue Jan 01 00:00:00 EST 2013 · Frontiers in Microbiology

DOI:https://doi.org/10.3389/fmicb.2013.00069· OSTI ID:1628083

Zhou, Yuzhen ^[1]; Dorchak, Alexandria E. ^[2]; Ragsdale, Stephen W. ^[2]

Univ. of Michigan, Ann Arbor, MI (United States). Univ. of Michigan Medical School Dept. of Biological Chemistry; DOE/OSTI
Univ. of Michigan, Ann Arbor, MI (United States). Univ. of Michigan Medical School Dept. of Biological Chemistry

Methyl-coenzyme M reductase (MCR) from methanogenic archaea catalyzes the rate-limiting and final step in methane biosynthesis. Using coenzyme B as the two-electron donor, MCR reduces methyl-coenzyme M (CH3-SCoM) to methane and the mixed disulfide, CoBS-SCoM. MCR contains an essential redox-active nickel tetrahydrocorphinoid cofactor, Coenzyme F430, at its active site. The active form of the enzyme (MCRred1) contains Ni(I)-F430. Rapid and efficient conversion of MCR to MCRred1 is important for elucidating the enzymatic mechanism, yet this reduction is difficult because the Ni(I) state is subject to oxidative inactivation. Furthermore, no in vitro methods have yet been described to convert Ni(II) forms into MCRred1. Since 1991, it has been known that MCRred1 from Methanothermobacter marburgensis can be generated in vivo when cells are purged with 100% H2. Here we show that purging cells or cell extracts with CO can also activate MCR. The rate of in vivo activation by CO is about 15 times faster than by H2 (130 and 8 min-1, respectively) and CO leads to twofold higher MCRred1 than H2. Unlike H2-dependent activation, which exhibits a 10-h lag time, there is no lag for CO-dependent activation. Based on cyanide inhibition experiments, carbon monoxide dehydrogenase is required for the CO-dependent activation. Formate, which also is a strong reductant, cannot activate MCR in M. marburgensis in vivo.

View Accepted Manuscript (DOE)

Research Organization:: Univ. of Michigan, Ann Arbor, MI (United States)

Sponsoring Organization:: USDOE Office of Science (SC)

Grant/Contract Number:: FG02-08ER15931

OSTI ID:: 1628083

Journal Information:: Frontiers in Microbiology, Journal Name: Frontiers in Microbiology Vol. 4; ISSN 1664-302X

Publisher:: Frontiers Research FoundationCopyright Statement

Country of Publication:: United States

Language:: English

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59 BASIC BIOLOGICAL SCIENCES
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