(Q44427736)

2 December 2017

title

Catalysis by methyl-coenzyme M reductase: a theoretical study for heterodisulfide product formation (English)

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2 December 2017

author

Vladimir Pelmenschikov

series ordinal

1

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2 December 2017

Per E M Siegbahn

2

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2 December 2017

publication date

1 May 2003

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Journal of Biological Inorganic Chemistry

2 December 2017

published in

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2 December 2017

volume

8

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2 December 2017

issue

6

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2 December 2017

page(s)

653-662

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https://scigraph.springernature.com/pub.10.1007/s00775-003-0461-8

2 December 2017

exact match

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cites work

Evidence that the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreonine phosphate is a product of the methylreductase reaction in Methanobacterium

1 reference

12 December 2020

Activation of methyl-SCoM reductase to high specific activity after treatment of whole cells with sodium sulfide

1 reference

12 December 2020

On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding

1 reference

12 December 2020

X-ray absorption and resonance Raman studies of methyl-coenzyme M reductase indicating that ligand exchange and macrocycle reduction accompany reductive activation.

1 reference

12 December 2020

The magnetic and electronic properties of Methanobacterium thermoautotrophicum (strain delta H) methyl coenzyme M reductase and its nickel tetrapyrrole cofactor F430. A low temperature magnetic circular dichroism study

1 reference

12 December 2020

The final step in methane formation. Investigations with highly purified methyl-CoM reductase (component C) from Methanobacterium thermoautotrophicum (strain Marburg).

1 reference

12 December 2020

H2: heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum. Composition and properties

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12 December 2020

The magnetic properties of the nickel cofactor F430 in the enzyme methyl-coenzyme M reductase of Methanobacterium thermoautotrophicum

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12 December 2020

Biochemistry of methanogenesis: a tribute to Marjory Stephenson. 1998 Marjory Stephenson Prize Lecture

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12 December 2020

Purified methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced to the nickel(I) oxidation state by titanium(III) citrate

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12 December 2020

Deconstructing F(430): quantum chemical perspectives of biological methanogenesis

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12 December 2020

A mechanism from quantum chemical studies for methane formation in methanogenesis

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12 December 2020

Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation

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12 December 2020

Density-functional exchange-energy approximation with correct asymptotic behavior

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12 December 2020

Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation

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12 December 2020

Cryoreduction of methyl-coenzyme M reductase: EPR characterization of forms, MCR(ox1) and MCR (red1)

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12 December 2020

Component C of the methylreductase system of Methanobacterium

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12 December 2020

Rapid ligand exchange in the MCRred1 form of methyl-coenzyme M reductase

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12 December 2020

Oxidative chemistry of nickel porphyrins

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12 December 2020

Purification of a cytochrome b containing H2:heterodisulfide oxidoreductase complex from membranes of Methanosarcina barkeri

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12 December 2020

Catalytic mechanism of matrix metalloproteinases: two-layered ONIOM study

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12 December 2020

Coordination and geometry of the nickel atom in active methyl-coenzyme M reductase from Methanothermobacter marburgensis as detected by X-ray absorption spectroscopy

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12 December 2020

Methane: small molecule, big impact

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12 December 2020

The enzyme at the end of the food chain

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12 December 2020

10.1007/S00775-003-0461-8

Identifiers

DOI

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2 December 2017

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