Electron transfer and conformation states in bovine cytochrome c oxidase.

about

Photoperturbation of the heme a3-CuB binuclear center of cytochrome c oxidase CO complex observed by Fourier transform infrared spectroscopy

P2860

Q34040408-740F32C4-57B3-470B-9252-F81F76CE0C06

P2860

Electron transfer and conformation states in bovine cytochrome c oxidase.

Item

http://www.wikidata.org/entity/Q54130747

description

1988 nî lūn-bûn

@nan

1988年の論文

@ja

1988年学术文章

@wuu

1988年学术文章

@zh-cn

1988年学术文章

@zh-hans

1988年学术文章

@zh-my

1988年学术文章

@zh-sg

1988年學術文章

@yue

1988年學術文章

@zh

1988年學術文章

@zh-hant

name

Electron transfer and conformation states in bovine cytochrome c oxidase.

@en

Electron transfer and conformation states in bovine cytochrome c oxidase.

@nl

type

Item

label

Electron transfer and conformation states in bovine cytochrome c oxidase.

@en

Electron transfer and conformation states in bovine cytochrome c oxidase.

@nl

prefLabel

Electron transfer and conformation states in bovine cytochrome c oxidase.

@en

Electron transfer and conformation states in bovine cytochrome c oxidase.

@nl

P1476

Electron transfer and conformation states in bovine cytochrome c oxidase.

@en

P2093

Alleyne T

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

Clague M

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

Conroy K

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

Wilson MT

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

el-Agez B

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

P2860

Redox-linked hydrogen bond strength changes in cytochrome a: implications for a cytochrome oxidase proton pump.

Cyanide inhibition of cytochrome c oxidase. A rapid-freeze e.p.r. investigation.

Spectroscopic analysis of the cytochrome c oxidase-cytochrome c complex: circular dichroism and magnetic circular dichroism measurements reveal change of cytochrome c heme geometry imposed by complex formation.

Functional intermediates in reaction of cytochrome oxidase with oxygen.

A plausible two-state model for cytochrome c oxidase

Cytochrome-c oxidase. Subunit structure and proton pumping.

A new redox loop formality involving metal-catalysed hydroxide-ion translocation. A hypothetical Cu loop mechanism for cytochrome oxidase.

The proton-pumping site of cytochrome c oxidase: a model of its structure and mechanism.

Zinc cytochrome c fluorescence as a probe for conformational changes in cytochrome c oxidase

The reaction of fully reduced cytochrome c oxidase with oxygen studied by flow-flash spectrophotometry at room temperature. Evidence for new pathways of electron transfer.

P304

167-176

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

P31

scholarly article

P356

10.1111/J.1749-6632.1988.TB35333.X

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

P478

550

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

P577

1988-01-01T00:00:00Z

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

P698

2854389

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

Electron transfer and conformation states in bovine cytochrome c oxidase.

about

P2860

P2860

Electron transfer and conformation states in bovine cytochrome c oxidase.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P478

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P478

P577

P698