Comparison of the structural and kinetic properties of the cytochrome c nitrite reductases from Escherichia coli, Wolinella succinogenes, Sulfurospirillum deleyianum and Desulfolvibrio desulfuricans

TA Clarke; AM Hemmings; B Burlat; JN Butt; Jeffrey Cole; DJ Richardson

doi:10.1042/BST0340143

Comparison of the structural and kinetic properties of the cytochrome c nitrite reductases from Escherichia coli, Wolinella succinogenes, Sulfurospirillum deleyianum and Desulfolvibrio desulfuricans

TA Clarke, AM Hemmings, B Burlat, JN Butt, Jeffrey Cole, DJ Richardson

Biosciences

Research output: Contribution to journal › Article

18 Citations (Scopus)

Abstract

The recent crystallographic characterization of NrfAs from Sulfurospirillum, deleyianum, Wolinella succinogenes, Escherichia coli and Desulfovibrio desulfuricans allows structurally conserved regions to be identified. Comparison of nitrite and sulphite reductase activities from different bacteria shows that the relative activities vary according to organism. By comparison of both amino acid sequences and structures, differences can be identified in the monomer-monomer interface and the active-site channel; these differences could be responsible for the observed variance in substrate activity and indicate that subtle changes in the NrfA structure may optimize the enzyme for different roles.

Original language	English
Pages (from-to)	143-145
Number of pages	3
Journal	Biochemical Society Transactions
Volume	34
DOIs	https://doi.org/10.1042/BST0340143
Publication status	Published - 1 Feb 2006

Keywords

active-site channel
NrfA
sequence alignment
cytochrome c
nitrite reductase
structural alignment

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10.1042/BST0340143

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title = "Comparison of the structural and kinetic properties of the cytochrome c nitrite reductases from Escherichia coli, Wolinella succinogenes, Sulfurospirillum deleyianum and Desulfolvibrio desulfuricans",

abstract = "The recent crystallographic characterization of NrfAs from Sulfurospirillum, deleyianum, Wolinella succinogenes, Escherichia coli and Desulfovibrio desulfuricans allows structurally conserved regions to be identified. Comparison of nitrite and sulphite reductase activities from different bacteria shows that the relative activities vary according to organism. By comparison of both amino acid sequences and structures, differences can be identified in the monomer-monomer interface and the active-site channel; these differences could be responsible for the observed variance in substrate activity and indicate that subtle changes in the NrfA structure may optimize the enzyme for different roles.",

keywords = "active-site channel, NrfA, sequence alignment, cytochrome c, nitrite reductase, structural alignment",

author = "TA Clarke and AM Hemmings and B Burlat and JN Butt and Jeffrey Cole and DJ Richardson",

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Clarke, TA, Hemmings, AM, Burlat, B, Butt, JN, Cole, J & Richardson, DJ 2006, 'Comparison of the structural and kinetic properties of the cytochrome c nitrite reductases from Escherichia coli, Wolinella succinogenes, Sulfurospirillum deleyianum and Desulfolvibrio desulfuricans', Biochemical Society Transactions, vol. 34, pp. 143-145. https://doi.org/10.1042/BST0340143

TY - JOUR

T1 - Comparison of the structural and kinetic properties of the cytochrome c nitrite reductases from Escherichia coli, Wolinella succinogenes, Sulfurospirillum deleyianum and Desulfolvibrio desulfuricans

AU - Clarke, TA

AU - Hemmings, AM

AU - Burlat, B

AU - Butt, JN

AU - Cole, Jeffrey

AU - Richardson, DJ

PY - 2006/2/1

Y1 - 2006/2/1

N2 - The recent crystallographic characterization of NrfAs from Sulfurospirillum, deleyianum, Wolinella succinogenes, Escherichia coli and Desulfovibrio desulfuricans allows structurally conserved regions to be identified. Comparison of nitrite and sulphite reductase activities from different bacteria shows that the relative activities vary according to organism. By comparison of both amino acid sequences and structures, differences can be identified in the monomer-monomer interface and the active-site channel; these differences could be responsible for the observed variance in substrate activity and indicate that subtle changes in the NrfA structure may optimize the enzyme for different roles.

AB - The recent crystallographic characterization of NrfAs from Sulfurospirillum, deleyianum, Wolinella succinogenes, Escherichia coli and Desulfovibrio desulfuricans allows structurally conserved regions to be identified. Comparison of nitrite and sulphite reductase activities from different bacteria shows that the relative activities vary according to organism. By comparison of both amino acid sequences and structures, differences can be identified in the monomer-monomer interface and the active-site channel; these differences could be responsible for the observed variance in substrate activity and indicate that subtle changes in the NrfA structure may optimize the enzyme for different roles.

KW - active-site channel

KW - NrfA

KW - sequence alignment

KW - cytochrome c

KW - nitrite reductase

KW - structural alignment

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U2 - 10.1042/BST0340143

DO - 10.1042/BST0340143

M3 - Article

C2 - 16417505

SN - 0300-5127

VL - 34

SP - 143

EP - 145

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

ER -

Comparison of the structural and kinetic properties of the cytochrome c nitrite reductases from Escherichia coli, Wolinella succinogenes, Sulfurospirillum deleyianum and Desulfolvibrio desulfuricans

Abstract

Keywords

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