(Q36715549)

15 August 2017

Design of a ruthenium-cytochrome c derivative to measure electron transfer to the initial acceptor in cytochrome c oxidase (English)

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15 August 2017

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Geren LM

1

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15 August 2017

Beasley JR

2

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15 August 2017

Fine BR

3

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15 August 2017

Saunders AJ

4

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15 August 2017

Hibdon S

5

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15 August 2017

Pielak GJ

6

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15 August 2017

Durham B

7

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15 August 2017

Millett F

8

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15 August 2017

language of work or name

English

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publication date

1 February 1995

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Journal of Biological Chemistry

15 August 2017

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15 August 2017

270

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15 August 2017

2466-2472

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15 August 2017

6

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Identification of the electron transfers in cytochrome oxidase that are coupled to proton-pumping

15 August 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Proton translocation in cytochrome c oxidase: redox linkage through proximal ligand exchange on cytochrome a3.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Coordination dynamics of heme-copper oxidases. The ligand shuttle and the control and coupling of electron transfer and proton translocation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Definition of the catalytic site of cytochrome c oxidase: specific ligands of heme a and the heme a3-CuB center

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochrome aa3 and cytochrome bo.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Multifrequency EPR evidence for a bimetallic center at the CuA site in cytochrome c oxidase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

The CuAsite of the caa3-type oxidase of Bacillus subtilis is a mixed-valence binuclear copper centre

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Use of specific lysine modifications to locate the reaction site of cytochrome c with cytochrome oxidase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Ionic strength dependence of the kinetics of electron transfer from bovine mitochondrial cytochrome c to bovine cytochrome c oxidase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Intracomplex electron transfer between ruthenium-cytochrome c derivatives and cytochrome c oxidase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Photoinduced electron transfer between cytochrome c peroxidase and yeast cytochrome c labeled at Cys 102 with (4-bromomethyl-4'-methylbipyridine)[bis(bipyridine)]ruthenium2+

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Photoinduced electron transfer between cytochrome c peroxidase and horse cytochrome c labeled at specific lysines with (dicarboxybipyridine)(bisbipyridine)ruthenium(II)

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Reaction of horse cytochrome c with the radical and the oxyferryl heme in cytochrome c peroxidase compound I.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Genetic engineering of redox donor sites: measurement of intracomplex electron transfer between ruthenium-65-cytochrome b5 and cytochrome c

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Intracomplex electron transfer between ruthenium-65-cytochrome b5 and position-82 variants of yeast iso-1-cytochrome c.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

The polypeptide composition of cytochrome oxidase from beef heart mitochondria.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Probing weakly polar interactions in cytochrome c

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Oxidation state-dependent conformational changes in cytochrome c

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Spectrum of horse-heart cytochrome c.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Laser flash photolysis studies of electron transfer between semiquinone and fully reduced free flavins and the cytochrome c-cytochrome oxidase complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Some properties of the redox components of cytochrome c oxidase and their interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Photoinduced electron transfer from tris(2,2'-bipyridyl)ruthenium to cytochrome c oxidase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Electron transfer between cytochrome a and copper A in cytochrome c oxidase: a perturbed equilibrium study

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Possible role of the mitochondrial outer membrane as an oncotic regulator of mitochondrial volume

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Interaction of cytochrome c with cytochrome c oxidase: an understanding of the high- to low-affinity transition

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

The steady-state kinetics of cytochrome c oxidation by cytochrome oxidase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Brownian dynamics of cytochrome c and cytochrome c peroxidase association

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

A comparative EPR investigation of the multicopper proteins nitrous-oxide reductase and cytochrome c oxidase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Identification of specific carboxylate groups on cytochrome c oxidase that are involved in binding cytochrome c

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Preparation and characterization of singly labeled ruthenium polypyridine cytochrome c derivatives

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Photoinduced electron-transfer kinetics of singly labeled ruthenium bis(bipyridine) dicarboxybipyridine cytochrome c derivatives

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Photoinduced electron transfer within complexes between plastocyanin and ruthenium bisbipyridine dicarboxybipyridine cytochrome c derivatives

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

The function of the Saccharomyces cerevisiae iso-1-cytochrome c gene is independent of the codon at invariant residue Phe82 when the gene is present on a low-copy-number vector

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Introduction of a disulfide bond into cytochrome c stabilizes a compact denatured state

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c with threonine: improved stability of the mutant protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Assignment of proton resonances, identification of secondary structural elements, and analysis of backbone chemical shifts for the C102T variant of yeast iso-1-cytochrome c and horse cytochrome c

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Evidence for modulation of the heme absorptions of cytochrome c oxidase by metal-metal interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Electron-tunneling pathways in cytochrome C

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Oxidative titrations of reduced cytochrome aa3: correlation of midpoint potentials and extinction coefficients observed at three major absorption bands

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

The oxidation-reduction potential of the copper signal in pigeon heart mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Heme-heme interaction in cytochrome oxidase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Ionic strength effects on cytochrome aa3 kinetics

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

The concept of high- and low-affinity reactions in bovine cytochrome c oxidase steady-state kinetics

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

The kinetics of cytochrome c oxidase. I. The system: cytochrome c-cytochrome oxidase-oxygen

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

Reduction of horse heart ferricytochrome c by bovine liver ferrocytochrome b5. Experimental and theoretical analysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.6.2466

21 January 2018

Identifiers

DOI

10.1074/JBC.270.6.2466

1 reference

15 August 2017

1 reference