Biochemical and spectroscopic studies of the electronic structure and reactivity of a methyl-Ni species formed on methyl-coenzyme M reductase. Academic Article uri icon


  • The enzyme methyl coenzyme M reductase (MCR) catalyzes the final step of methane production by methanogenic organisms. The active site contains a Ni-macrocyclic complex, F430, in which the Ni is in the 1+ oxidation state in the active form, MCRred1. We describe the preparation and spectroscopic characterization of a Ni-methyl species, denoted MCRMe, generated from MCRred1 by reaction with CH3I. EPR and 13C, 1,2H pulsed ENDOR spectra of methyl isotopologues (CH3, CD3, 13CH3) umambiguously establish the presence of CH3-Ni(III) moiety. They explain why both MCRred1 and MCRMe have dx2-y2 odd-electrons although formally having Ni(I) in the former and Ni(III) in the latter. The simple MO description further gives a simple explanation to the small transfer of spin density (-1%) from Ni to methyl. The MCRME species undergoes conversion to methane and to methyl-SCoM, indicating its catalytic competence as an intermediate in methanogenesis. Copyright © 2007 American Chemical Society.

published proceedings

  • J Am Chem Soc

altmetric score

  • 1

author list (cited authors)

  • Dey, M., Telser, J., Kunz, R. C., Lees, N. S., Ragsdale, S. W., & Hoffman, B. M

citation count

  • 53

complete list of authors

  • Dey, Mishtu||Telser, Joshua||Kunz, Ryan C||Lees, Nicholas S||Ragsdale, Stephen W||Hoffman, Brian M

publication date

  • August 2007