(Q46868416)

26 December 2017

title

Defining the proton entry point in the bacterial respiratory nitric-oxide reductase (English)

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26 December 2017

author

Nicholas Watmough

5

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26 December 2017

author name string

Ulrika Flock

1

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26 December 2017

Faye H Thorndycroft

2

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26 December 2017

Andrey D Matorin

3

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26 December 2017

David J Richardson

4

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26 December 2017

Pia Adelroth

6

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26 December 2017

language of work or name

English

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publication date

3 December 2007

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26 December 2017

Journal of Biological Chemistry

number of pages

7

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based on heuristic

inferred from page(s)

published in

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26 December 2017

volume

283

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26 December 2017

issue

7

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26 December 2017

page(s)

3839-3845

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26 December 2017

Nitric oxide in bacteria: synthesis and consumption

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

Nitric oxide reductases of prokaryotes with emphasis on the respiratory, heme-copper oxidase type

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

Cytochrome oxidase evolved by tinkering with denitrification enzymes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

The active site of the bacterial nitric oxide reductase is a dinuclear iron center

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

A new assay for nitric oxide reductase reveals two conserved glutamate residues form the entrance to a proton-conducting channel in the bacterial enzyme.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

Proton and electron pathways in the bacterial nitric oxide reductase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

Two conserved glutamates in the bacterial nitric oxide reductase are essential for activity but not assembly of the enzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

Cytochrome cb-type nitric oxide reductase with cytochrome c oxidase activity from Paracoccus denitrificans ATCC 35512

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

Electron/proton coupling in bacterial nitric oxide reductase during reduction of oxygen

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

Proton transfer in bacterial nitric oxide reductase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

Wolinella succinogenes quinol:fumarate reductase-2.2-A resolution crystal structure and the E-pathway hypothesis of coupled transmembrane proton and electron transfer

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

The MCD and EPR of the heme centers of nitric oxide reductase from Pseudomonas stutzeri: evidence that the enzyme is structurally related to the heme-copper oxidases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

On the role of the K-proton transfer pathway in cytochrome c oxidase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

Marcus rate theory applied to enzymatic proton transfer

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

A theoretical study on nitric oxide reductase activity in a ba(3)-type heme-copper oxidase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

Existence of a proton transfer chain in bacteriorhodopsin: participation of Glu-194 in the release of protons to the extracellular surface

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

Proton binding within a membrane protein by a protonated water cluster

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

The cbb3-type cytochrome c oxidase from Rhodobacter sphaeroides, a proton-pumping heme-copper oxidase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

VMD: visual molecular dynamics

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

Comparative genomics and site-directed mutagenesis support the existence of only one input channel for protons in the C-family (cbb3 oxidase) of heme-copper oxygen reductases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M704615200

21 January 2018

Identifiers

DOI

10.1074/JBC.M704615200

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26 December 2017

PubMed ID

18056717

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26 December 2017