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

TA Clarke; AM Hemmings; B Burlat; JN Butt; JA 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 Desulfovibrio desulfuricans

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

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

21 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
Issue number	1
DOIs	https://doi.org/10.1042/BST0340143
Publication status	Published - 2006

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10.1042/BST0340143

Cite this

Clarke, TA., Hemmings, AM., Burlat, B., Butt, JN., Cole, JA., & Richardson, DJ. (2006). Comparison of the structural and kinetic properties of the cytochrome c nitrite reductases from Escherichia coli, Wolinella succinogenes, Sulfurospirillum deleyianum and Desulfovibrio desulfuricans. Biochemical Society Transactions, 34(1), 143-145. https://doi.org/10.1042/BST0340143

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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.",

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Clarke, TA , Hemmings, AM, Burlat, B, Butt, JN, Cole, JA & Richardson, DJ 2006, 'Comparison of the structural and kinetic properties of the cytochrome c nitrite reductases from Escherichia coli, Wolinella succinogenes, Sulfurospirillum deleyianum and Desulfovibrio desulfuricans', Biochemical Society Transactions, vol. 34, no. 1, pp. 143-145. https://doi.org/10.1042/BST0340143

Comparison of the structural and kinetic properties of the cytochrome c nitrite reductases from Escherichia coli, Wolinella succinogenes, Sulfurospirillum deleyianum and Desulfovibrio desulfuricans. / Clarke, TA ; Hemmings, AM; Burlat, B et al.

In: Biochemical Society Transactions, Vol. 34, No. 1, 2006, p. 143-145.

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

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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.

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DO - 10.1042/BST0340143

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