Identification of the iron-sulfur center in trimethylamine dehydrogenase. - Wikidata - awgldk - TriplyDB

Identification of the iron-sulfur center in trimethylamine dehydrogenase.

Identification of the iron-sulfur center in trimethylamine dehydrogenase.

http://www.wikidata.org/entity/Q37581737

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Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase in catalysis Structural Comparisons of Apo- and Metalated Three-Stranded Coiled Coils Clarify Metal Binding Determinants in Thiolate Containing Designed Peptides Mechanistic studies on the dehydrogenases of methylotrophic bacteria. 2. Kinetic studies on the intramolecular electron transfer in trimethylamine and dimethylamine dehydrogenase Identification of iron-sulfur centers in the iron-molybdenum proteins of nitrogenase Electron transfer and conformational change in complexes of trimethylamine dehydrogenase and electron transferring flavoprotein.The reaction of trimethylamine dehydrogenase with electron transferring flavoprotein.Cluster characterization in iron-sulfur proteins by magnetic circular dichroism Bacterial iron-sulfur proteins.Characterization of the second prosthetic group of the flavoenzyme NADH-acceptor reductase (component C) of the methane mono-oxygenase from Methylococcus capsulatus (Bath).Mechanistic studies on the dehydrogenases of methylotrophic bacteria. 1. The influence of substrate binding to reduced trimethylamine dehydrogenase on the intramolecular electron transfer between its prosthetic groups.Reductive half-reaction of the H172Q mutant of trimethylamine dehydrogenase: evidence against a carbanion mechanism and assignment of kinetically influential ionizations in the enzyme-substrate complex.Identity of the subunits and the stoicheiometry of prosthetic groups in trimethylamine dehydrogenase and dimethylamine dehydrogenase.Microcoulometric analysis of trimethylamine dehydrogenase The interaction of trimethylamine dehydrogenase and electron-transferring flavoprotein.

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P2860

Identification of the iron-sulfur center in trimethylamine dehydrogenase.

http://www.wikidata.org/entity/Q37581737

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on February 1977

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Identification of the iron-sulfur center in trimethylamine dehydrogenase.

@en

Identification of the iron-sulfur center in trimethylamine dehydrogenase.

@nl

type

label

Identification of the iron-sulfur center in trimethylamine dehydrogenase.

@en

Identification of the iron-sulfur center in trimethylamine dehydrogenase.

@nl

prefLabel

Identification of the iron-sulfur center in trimethylamine dehydrogenase.

@en

Identification of the iron-sulfur center in trimethylamine dehydrogenase.

@nl

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Identification of the iron-sulfur center in trimethylamine dehydrogenase.

@en

P2093

Hill CL

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Holm RH

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Singer TP

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Steenkamp DJ

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P2860

Trimethylamine dehydrogenase from a methylotrophic bacterium. I. Isolation and steady-state kinetics

On the iron-sulfur cluster in hydrogenase from Clostridium pasteurianum W5.

Iron-sulfur proteins: structure and function.

Iron-sulfur components of succinate dehydrogenase: stoichiometry and kinetic behavior in activated preparations.

X-ray structural studies of ferredoxin and related electron carriers.

The role of an iron-sulfur center and siroheme in spinach nitrite reductase.

Thermodynamic and EPR characteristics of a HiPIP-type iron-sulfur center in the succinate dehydrogenase of the respiratory chain.

Purification and properties of the trimethylamine dehydrogenase of bacterium 4B6.

Synthetic analogs of the active sites of iron-sulfur proteins. VII. Ligand substitution reactions of the tetranuclear clusters (Fe4S4(SR)4)2- and the structure of ((CH3)4N)2(Fe4S4(SC6H5)4).

Synthetic analogs of the active sites of iron-sulfur proteins. VI. Spectral and redox characteristics of the tetranuclear clusters (Fe4S4(SR)4).2-.

P304

547-551

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scholarly article

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10.1073/PNAS.74.2.547

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2

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74

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1977-02-01T00:00:00Z

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22871025

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265519

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392327

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