Cytochrome c nitrite reductase: from structural to physicochemical analysis

B Burlat; JD Gwyer; S Poock; TA Clarke; JA Cole; AM Hemmings; MR Cheesman; JN Butt; DJ Richardson

doi:10.1042/BST0330137

Cytochrome c nitrite reductase: from structural to physicochemical analysis

B Burlat, JD Gwyer, S Poock, TA Clarke, JA Cole, AM Hemmings, MR Cheesman, JN Butt, DJ Richardson

Research output: Contribution to journal › Article › peer-review

22 Citations (Scopus)

Abstract

The recent structural characterization of the NrfA from Escherichia coli provides a framework to rationalize the spectroscopic and functional properties of this enzyme. Analyses by EPR and magnetic CD spectroscopies have been complemented by protein-film voltammetry and these are discussed in relation to the essential structural features of the enzyme.

Original language	English
Pages (from-to)	137-140
Number of pages	4
Journal	Biochemical Society Transactions
Volume	33
Issue number	1
DOIs	https://doi.org/10.1042/BST0330137
Publication status	Published - 2005

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10.1042/BST0330137

Cite this

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title = "Cytochrome c nitrite reductase: from structural to physicochemical analysis",

abstract = "The recent structural characterization of the NrfA from Escherichia coli provides a framework to rationalize the spectroscopic and functional properties of this enzyme. Analyses by EPR and magnetic CD spectroscopies have been complemented by protein-film voltammetry and these are discussed in relation to the essential structural features of the enzyme.",

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AU - Burlat, B

AU - Gwyer, JD

AU - Poock, S

AU - Clarke, TA

AU - Cole, JA

AU - Hemmings, AM

AU - Cheesman, MR

AU - Butt, JN

AU - Richardson, DJ

PY - 2005

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AB - The recent structural characterization of the NrfA from Escherichia coli provides a framework to rationalize the spectroscopic and functional properties of this enzyme. Analyses by EPR and magnetic CD spectroscopies have been complemented by protein-film voltammetry and these are discussed in relation to the essential structural features of the enzyme.

U2 - 10.1042/BST0330137

DO - 10.1042/BST0330137

M3 - Article

VL - 33

SP - 137

EP - 140

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

SN - 0300-5127

IS - 1

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