Intermediates in the catalytic cycle of methyl coenzyme M reductase: Isotope exchange is consistent with formation of a σ-Alkane-Nickel Complex

Silvan Scheller; Meike Goenrich; Stefan Mayr; Rudolf K. Thauer; Bernhard Jaun

doi:10.1002/anie.201003214

Intermediates in the catalytic cycle of methyl coenzyme M reductase: Isotope exchange is consistent with formation of a σ-Alkane-Nickel Complex

Silvan Scheller^*, Meike Goenrich, Stefan Mayr, Rudolf K. Thauer, Bernhard Jaun

^*Corresponding author for this work

Not published at Aalto University

Research output: Contribution to journal › Article › Scientific › peer-review

37 Citations (Scopus)

Abstract

The key nickel enzyme for methanogenesis (MCR) catalyzes the formation of CH₃D and CH₂D₂ in a deuterated medium. CH ₂D₂ is formed by an exchange of deuterium into the S-methyl group of the substrate. Deuterium is incorporated at both carbon atoms of the S-ethyl group of ethyl coenzyme M, and a ¹³C label is rapidly scrambled within the ethyl group (see scheme). Thus, at least one intermediate is formed and the isotope exchange pattern is consistent with formation of a σ-alkane-nickel complex.

Original language	English
Pages (from-to)	8112-8115
Number of pages	4
Journal	Angewandte Chemie
Volume	49
Issue number	44
DOIs	https://doi.org/10.1002/anie.201003214
Publication status	Published - 25 Oct 2010
MoE publication type	A1 Journal article-refereed

Keywords

σ-alkane ligands
C-H activation
Isotope exchange
Methyl coenzyme M reductase
Nickel enzymes

Access to Document

10.1002/anie.201003214

Cite this

@article{fe74005c236d459e87c455083f59a369,

title = "Intermediates in the catalytic cycle of methyl coenzyme M reductase: Isotope exchange is consistent with formation of a σ-Alkane-Nickel Complex",

abstract = "The key nickel enzyme for methanogenesis (MCR) catalyzes the formation of CH3D and CH2D2 in a deuterated medium. CH 2D2 is formed by an exchange of deuterium into the S-methyl group of the substrate. Deuterium is incorporated at both carbon atoms of the S-ethyl group of ethyl coenzyme M, and a 13C label is rapidly scrambled within the ethyl group (see scheme). Thus, at least one intermediate is formed and the isotope exchange pattern is consistent with formation of a σ-alkane-nickel complex.",

keywords = "σ-alkane ligands, C-H activation, Isotope exchange, Methyl coenzyme M reductase, Nickel enzymes",

author = "Silvan Scheller and Meike Goenrich and Stefan Mayr and Thauer, {Rudolf K.} and Bernhard Jaun",

year = "2010",

month = oct,

day = "25",

doi = "10.1002/anie.201003214",

language = "English",

volume = "49",

pages = "8112--8115",

journal = "Angewandte Chemie",

issn = "1433-7851",

number = "44",

}

Intermediates in the catalytic cycle of methyl coenzyme M reductase : Isotope exchange is consistent with formation of a σ-Alkane-Nickel Complex. / Scheller, Silvan; Goenrich, Meike; Mayr, Stefan; Thauer, Rudolf K.; Jaun, Bernhard.

In: Angewandte Chemie, Vol. 49, No. 44, 25.10.2010, p. 8112-8115.

Research output: Contribution to journal › Article › Scientific › peer-review

TY - JOUR

T1 - Intermediates in the catalytic cycle of methyl coenzyme M reductase

T2 - Isotope exchange is consistent with formation of a σ-Alkane-Nickel Complex

AU - Scheller, Silvan

AU - Goenrich, Meike

AU - Mayr, Stefan

AU - Thauer, Rudolf K.

AU - Jaun, Bernhard

PY - 2010/10/25

Y1 - 2010/10/25

N2 - The key nickel enzyme for methanogenesis (MCR) catalyzes the formation of CH3D and CH2D2 in a deuterated medium. CH 2D2 is formed by an exchange of deuterium into the S-methyl group of the substrate. Deuterium is incorporated at both carbon atoms of the S-ethyl group of ethyl coenzyme M, and a 13C label is rapidly scrambled within the ethyl group (see scheme). Thus, at least one intermediate is formed and the isotope exchange pattern is consistent with formation of a σ-alkane-nickel complex.

AB - The key nickel enzyme for methanogenesis (MCR) catalyzes the formation of CH3D and CH2D2 in a deuterated medium. CH 2D2 is formed by an exchange of deuterium into the S-methyl group of the substrate. Deuterium is incorporated at both carbon atoms of the S-ethyl group of ethyl coenzyme M, and a 13C label is rapidly scrambled within the ethyl group (see scheme). Thus, at least one intermediate is formed and the isotope exchange pattern is consistent with formation of a σ-alkane-nickel complex.

KW - σ-alkane ligands

KW - C-H activation

KW - Isotope exchange

KW - Methyl coenzyme M reductase

KW - Nickel enzymes

UR - http://www.scopus.com/inward/record.url?scp=78249249257&partnerID=8YFLogxK

U2 - 10.1002/anie.201003214

DO - 10.1002/anie.201003214

M3 - Article

C2 - 20857468

AN - SCOPUS:78249249257

VL - 49

SP - 8112

EP - 8115

JO - Angewandte Chemie

JF - Angewandte Chemie

SN - 1433-7851

IS - 44

ER -

Intermediates in the catalytic cycle of methyl coenzyme M reductase: Isotope exchange is consistent with formation of a σ-Alkane-Nickel Complex

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this