Structural analysis of a Ni-methyl species in methyl-coenzyme M reductase from methanothermobacter marburgensis

Peder E. Cedervall; Mishtu Dey; Xianghui Li; Ritimukta Sarangi; Britt Hedman; Stephen W. Ragsdale; Carrie M. Wilmot

doi:10.1021/ja110492p

Structural analysis of a Ni-methyl species in methyl-coenzyme M reductase from methanothermobacter marburgensis

Peder E. Cedervall, Mishtu Dey, Xianghui Li, Ritimukta Sarangi, Britt Hedman, Stephen W. Ragsdale, Carrie M. Wilmot

Chemical and Structural Biology (BMBB)

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

40 Scopus citations

Abstract

We present the 1.2 Å resolution X-ray crystal structure of a Ni-methyl species that is a proposed catalytic intermediate in methyl-coenzyme M reductase (MCR), the enzyme that catalyzes the biological formation of methane. The methyl group is situated 2.1 Å proximal of the Ni atom of the MCR coenzyme F₄₃₀. A rearrangement of the substrate channel has been posited to bring together substrate species, but Ni(III)-methyl formation alone does not lead to any observable structural changes in the channel.

Original language	English (US)
Pages (from-to)	5626-5628
Number of pages	3
Journal	Journal of the American Chemical Society
Volume	133
Issue number	15
DOIs	https://doi.org/10.1021/ja110492p
State	Published - Apr 20 2011

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title = "Structural analysis of a Ni-methyl species in methyl-coenzyme M reductase from methanothermobacter marburgensis",

abstract = "We present the 1.2 {\AA} resolution X-ray crystal structure of a Ni-methyl species that is a proposed catalytic intermediate in methyl-coenzyme M reductase (MCR), the enzyme that catalyzes the biological formation of methane. The methyl group is situated 2.1 {\AA} proximal of the Ni atom of the MCR coenzyme F430. A rearrangement of the substrate channel has been posited to bring together substrate species, but Ni(III)-methyl formation alone does not lead to any observable structural changes in the channel.",

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T1 - Structural analysis of a Ni-methyl species in methyl-coenzyme M reductase from methanothermobacter marburgensis

AU - Cedervall, Peder E.

AU - Dey, Mishtu

AU - Li, Xianghui

AU - Sarangi, Ritimukta

AU - Hedman, Britt

AU - Ragsdale, Stephen W.

AU - Wilmot, Carrie M.

PY - 2011/4/20

Y1 - 2011/4/20

N2 - We present the 1.2 Å resolution X-ray crystal structure of a Ni-methyl species that is a proposed catalytic intermediate in methyl-coenzyme M reductase (MCR), the enzyme that catalyzes the biological formation of methane. The methyl group is situated 2.1 Å proximal of the Ni atom of the MCR coenzyme F430. A rearrangement of the substrate channel has been posited to bring together substrate species, but Ni(III)-methyl formation alone does not lead to any observable structural changes in the channel.

AB - We present the 1.2 Å resolution X-ray crystal structure of a Ni-methyl species that is a proposed catalytic intermediate in methyl-coenzyme M reductase (MCR), the enzyme that catalyzes the biological formation of methane. The methyl group is situated 2.1 Å proximal of the Ni atom of the MCR coenzyme F430. A rearrangement of the substrate channel has been posited to bring together substrate species, but Ni(III)-methyl formation alone does not lead to any observable structural changes in the channel.

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DO - 10.1021/ja110492p

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JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 15

ER -

Structural analysis of a Ni-methyl species in methyl-coenzyme M reductase from methanothermobacter marburgensis

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