Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase in catalysis

Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase in catalysis

Item
http://www.wikidata.org/entity/Q24534826
Expression of human electron transfer flavoprotein-ubiquinone oxidoreductase from a baculovirus vector: kinetic and spectral characterization of the human proteinMechanistic studies on the dehydrogenases of methylotrophic bacteria. 2. Kinetic studies on the intramolecular electron transfer in trimethylamine and dimethylamine dehydrogenaseThe reaction of trimethylamine dehydrogenase with electron transferring flavoprotein.Bacterial iron-sulfur proteins.The flavinylation reaction of trimethylamine dehydrogenase. Analysis by directed mutagenesis and electrospray mass spectrometry.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 dehydrogenaseFlavinylation in wild-type trimethylamine dehydrogenase and differentially charged mutant enzymes: a study of the protein environment around the N1 of the flavin isoalloxazine.Deuterium isotope effects during carbon-hydrogen bond cleavage by trimethylamine dehydrogenase. Implications for mechanism and vibrationally assisted hydrogen tunneling in wild-type and mutant enzymes.Optimizing the Michaelis complex of trimethylamine dehydrogenase: identification of interactions that perturb the ionization of substrate and facilitate catalysis with trimethylamine base.The catalytic mechanism of 2-oxoacid:ferredoxin oxidoreductases from Halobacterium halobium. One-electron transfer at two distinct steps of the catalytic cycle.
P2860

Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase in catalysis

Item
http://www.wikidata.org/entity/Q24534826
description
1978 nî lūn-bûn
@nan
1978 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1978 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1978年の論文
@ja
1978年論文
@yue
1978年論文
@zh-hant
1978年論文
@zh-hk
1978年論文
@zh-mo
1978年論文
@zh-tw
1978年论文
@wuu
name
Participation of the iron-sulp ...... ine dehydrogenase in catalysis
@ast
Participation of the iron-sulp ...... ine dehydrogenase in catalysis
@en
Participation of the iron-sulp ...... ine dehydrogenase in catalysis
@en-gb
Participation of the iron-sulp ...... ine dehydrogenase in catalysis
@nl
type
label
Participation of the iron-sulp ...... ine dehydrogenase in catalysis
@ast
Participation of the iron-sulp ...... ine dehydrogenase in catalysis
@en
Participation of the iron-sulp ...... ine dehydrogenase in catalysis
@en-gb
Participation of the iron-sulp ...... ine dehydrogenase in catalysis
@nl
prefLabel
Participation of the iron-sulp ...... ine dehydrogenase in catalysis
@ast
Participation of the iron-sulp ...... ine dehydrogenase in catalysis
@en
Participation of the iron-sulp ...... ine dehydrogenase in catalysis
@en-gb
Participation of the iron-sulp ...... ine dehydrogenase in catalysis
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P932
P356
P1433
P1476
Participation of the iron-sulp ...... ine dehydrogenase in catalysis
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P932