Elucidating the process of activation of methyl-coenzyme M reductase

Divya Prakash, Yonnie Wu, Sang Jin Suh, Evert C. Duin

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

Methyl-coenzymeMreductase (MCR) catalyzes the reversible reduction of methyl-coenzyme M(CH3-S-CoM) and coenzyme B (HS-CoB) to methane and heterodisulfide CoM-S-S-CoB (HDS). MCR contains the hydroporphinoid nickel complex coenzyme F430 in its active site, and the Ni center has to be in its Ni(I) valence state for the enzyme to be active. Until now, no in vitro method that fully converted the inactive MCRsilent-Ni(II) form to the active MCRred1-Ni(I) form has been described. With the potential use of recombinant MCR in the production of biofuels and the need to better understand this enzyme and its activation process, we studied its activation under nonturnover conditions and achieved full MCR activation in the presence of dithiothreitol and protein components A2, an ATP carrier, and A3a. It was found that the presence of HDS promotes the inactivation of MCRred1, which makes it essential that the activation process is isolated from the methane formation assay, which tends to result in minimal activation rates. Component A3a is a multienzyme complex that includes the mcrC gene product, an Fe-protein homolog, an iron-sulfur flavoprotein, and protein components involved in electron bifurcation. A hypothetical model for the cellular activation process of MCR is presented.

Original languageEnglish (US)
Pages (from-to)2491-2498
Number of pages8
JournalJournal of bacteriology
Volume196
Issue number13
DOIs
StatePublished - Jan 1 2014

Fingerprint

Methane
Multienzyme Complexes
Iron-Sulfur Proteins
Flavoproteins
Enzyme Activation
Biofuels
Dithiothreitol
Nickel
varespladib methyl
Catalytic Domain
Proteins
Adenosine Triphosphate
Electrons
Enzymes
methyl coenzyme M reductase
In Vitro Techniques
factor F430
12-aza-13-carboxy-14-hydroxy-11-oxo-3,4-dithiapentadecanesulfonic acid 14-phosphate
methyl coenzyme M
7-mercaptoheptanoylthreonine phosphate

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

Cite this

Prakash, Divya ; Wu, Yonnie ; Suh, Sang Jin ; Duin, Evert C. / Elucidating the process of activation of methyl-coenzyme M reductase. In: Journal of bacteriology. 2014 ; Vol. 196, No. 13. pp. 2491-2498.
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Elucidating the process of activation of methyl-coenzyme M reductase. / Prakash, Divya; Wu, Yonnie; Suh, Sang Jin; Duin, Evert C.

In: Journal of bacteriology, Vol. 196, No. 13, 01.01.2014, p. 2491-2498.

Research output: Contribution to journalArticle

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