Facilitated intramolecular electron transfer in cytochrome bo-type ubiquinol oxidase initiated upon reaction of the fully reduced enzyme with dioxygen (Q72716857)

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scientific article published on 01 September 1994

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English	Facilitated intramolecular electron transfer in cytochrome bo-type ubiquinol oxidase initiated upon reaction of the fully reduced enzyme with dioxygen	scientific article published on 01 September 1994

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28 October 2019

Facilitated intramolecular electron transfer in cytochrome bo-type ubiquinol oxidase initiated upon reaction of the fully reduced enzyme with dioxygen (English)

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28 October 2019

author name string

Orii Y

1

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28 October 2019

Mogi T

2

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28 October 2019

Kawasaki M

3

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28 October 2019

Anraku Y

4

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publication date

1 September 1994

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28 October 2019

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28 October 2019

352

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28 October 2019

2

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28 October 2019

151-154

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28 October 2019

Cytochrome o (bo) is a proton pump in Paracoccus denitrificans and Escherichia coli

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2900939-2

21 January 2018

Properties of the two terminal oxidases of Escherichia coli

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2900939-2

21 January 2018

Molecular structure of a heme-copper redox center of the Escherichia coli ubiquinol oxidase: evidence and model

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2900939-2

21 January 2018

Structural features of cytochrome oxidase

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2900939-2

21 January 2018

Some recent advances relating to prokaryotic cytochrome c reductases and cytochrome c oxidases

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2900939-2

21 January 2018

Intermediates in the reaction of reduced cytochrome oxidase with dioxygen

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2900939-2

21 January 2018

Immediate reduction of cytochrome c by photoexcited NADH: reaction mechanism as revealed by flow-flash and rapid-scan studies

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2900939-2

21 January 2018

Structure of the heme-copper binuclear center of the cytochrome bo complex of Escherichia coli: EPR and Fourier transform infrared spectroscopic studies.

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2900939-2

21 January 2018

Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2900939-2

21 January 2018

Flow-flash study of the reaction between cytochrome bo and oxygen

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2900939-2

21 January 2018

The low-spin heme site of cytochrome o from Escherichia coli is promiscuous with respect to heme type.

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2900939-2

21 January 2018

Intramolecular electron transfer in cytochrome o of Escherichia coli: events following the photolysis of fully and partially reduced CO-bound forms of the bo3 and oo3 enzymes.

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2900939-2

21 January 2018

Heme O biosynthesis in Escherichia coli: the cyoE gene in the cytochrome bo operon encodes a protoheme IX farnesyltransferase

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2900939-2

21 January 2018

Oxygen activation and the conservation of energy in cell respiration

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2900939-2

21 January 2018

STUDIES ON CYTOCHROME A. 13. INTERPRETATION OF THE ANOMALOUS SPECTRAL BEHAVIORS OF CYTOCHROME A

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2900939-2

21 January 2018

Flash photolysis of the carbon monoxide compounds of wild-type and mutant variants of cytochrome bo from Escherichia coli

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2900939-2

21 January 2018

Spectroscopic characterization of mutants supports the assignment of histidine-419 as the axial ligand of heme o in the binuclear center of the cytochrome bo ubiquinol oxidase from Escherichia coli.

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2900939-2

21 January 2018

The high-spin cytochrome o' component of the cytochrome bo-type quinol oxidase in membranes from Escherichia coli: formation of the primary oxygenated species at low temperatures is characterized by a slow 'on' rate and low dissociation constant.

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2894%2900939-2

21 January 2018

Identifiers

10.1016/0014-5793(94)00939-2

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28 October 2019

1 reference

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28 October 2019

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