Dissecting the pattern of proton release from partial process involved in ubihydroquinone oxidation in the Q-cycle.

about

Dissecting the pattern of proton release from partial process involved in ubihydroquinone oxidation in the Q-cycle.

Item

http://www.wikidata.org/entity/Q52329906

description

2018 nî lūn-bûn

@nan

2018年の論文

@ja

2018年学术文章

@wuu

2018年学术文章

@zh

2018年学术文章

@zh-cn

2018年学术文章

@zh-hans

2018年学术文章

@zh-my

2018年学术文章

@zh-sg

2018年學術文章

@yue

2018年學術文章

@zh-hant

name

Dissecting the pattern of prot ...... none oxidation in the Q-cycle.

@en

Dissecting the pattern of prot ...... none oxidation in the Q-cycle.

@nl

type

Item

label

Dissecting the pattern of prot ...... none oxidation in the Q-cycle.

@en

Dissecting the pattern of prot ...... none oxidation in the Q-cycle.

@nl

prefLabel

Dissecting the pattern of prot ...... none oxidation in the Q-cycle.

@en

Dissecting the pattern of prot ...... none oxidation in the Q-cycle.

@nl

P1476

Dissecting the pattern of prot ...... none oxidation in the Q-cycle.

@en

P2093

Antony R Crofts

http://www.w3.org/2001/XMLSchema#string

Charles A Wilson

http://www.w3.org/2001/XMLSchema#string

P2860

Possible molecular mechanisms of the protonmotive function of cytochrome systems

Mechanism of ubiquinol oxidation by the bc(1) complex: role of the iron sulfur protein and its mobility.

Photoinduced electron transfer between the Rieske iron-sulfur protein and cytochrome c(1) in the Rhodobacter sphaeroides cytochrome bc(1) complex. Effects of pH, temperature, and driving force.

Modifications of protein environment of the [2Fe-2S] cluster of the bc1 complex: effects on the biophysical properties of the rieske iron-sulfur protein and on the kinetics of the complex.

Pathways for proton release during ubihydroquinone oxidation by the bc(1) complex.

NMR investigations of the Rieske protein from Thermus thermophilus support a coupled proton and electron transfer mechanism.

Integration of energy and electron transfer processes in the photosynthetic membrane of Rhodobacter sphaeroides.

Steered molecular dynamics simulation of the Rieske subunit motion in the cytochrome bc(1) complex.

THE ROLE OF THE QUINONE POOL IN THE CYCLIC ELECTRON-TRANSFER CHAIN OF RHODOPSEUDOMONAS SPHAEROIDES: A MODIFIED Q-CYCLE MECHANISM

Proton-coupled electron transfer at the Qo-site of the bc1 complex controls the rate of ubihydroquinone oxidation.

P304

531-543

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1016/J.BBABIO.2018.03.016

http://www.w3.org/2001/XMLSchema#string

P433

http://www.w3.org/2001/XMLSchema#string

P478

1859

http://www.w3.org/2001/XMLSchema#string

P577

2018-04-03T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

29625088

http://www.w3.org/2001/XMLSchema#string

P932

5955396

http://www.w3.org/2001/XMLSchema#string