The tetraheme cytochrome c NrfH is required to anchor the cytochrome c nitrite reductase (NrfA) in the membrane of Wolinella succinogenes. (Q30769137)

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3 December 2019

title

The tetraheme cytochrome c NrfH is required to anchor the cytochrome c nitrite reductase (NrfA) in the membrane of Wolinella succinogenes (English)

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3 December 2019

1

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3 December 2019

author name string

R Pisa

2

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3 December 2019

T Stein

3

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3 December 2019

R Eichler

4

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3 December 2019

O Klimmek

5

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3 December 2019

R Gross

6

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3 December 2019

language of work or name

English

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publication date

1 November 2001

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3 December 2019

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3 December 2019

volume

268

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3 December 2019

page(s)

5776-5782

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3 December 2019

issue

22

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A NapC/NirT-type cytochrome c (NrfH) is the mediator between the quinone pool and the cytochrome c nitrite reductase of Wolinella succinogenes.

3 December 2019

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1 reference

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Cytochrome c nitrite reductase from Wolinella succinogenes. Structure at 1.6 A resolution, inhibitor binding, and heme-packing motifs

21 January 2018

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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A periplasmic flavoprotein in Wolinella succinogenes that resembles the fumarate reductase of Shewanella putrefaciens.

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The nirSTBM region coding for cytochrome cd1-dependent nitrite respiration of Pseudomonas stutzeri consists of a cluster of mono-, di-, and tetraheme proteins

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Cloning and sequence of cymA, a gene encoding a tetraheme cytochrome c required for reduction of iron(III), fumarate, and nitrate by Shewanella putrefaciens MR-1

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Ammonia-forming cytochrome c nitrite reductase from Sulfurospirillum deleyianum is a tetraheme protein: new aspects of the molecular composition and spectroscopic properties

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Involvement of products of the nrfEFG genes in the covalent attachment of haem c to a novel cysteine-lysine motif in the cytochrome c552 nitrite reductase from Escherichia coli

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Spectroscopic characterization of a novel multiheme c-type cytochrome widely implicated in bacterial electron transport

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Purification and magneto-optical spectroscopic characterization of cytoplasmic membrane and outer membrane multiheme c-type cytochromes from Shewanella frigidimarina NCIMB400

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