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

2006/01/20 by Thomas A. Clarke, T.A. Clarke, A.M. Hemmings +9 · 2 citations
Biochemistry, Genetics and Molecular Biology · Energy · Environmental Science · #Arsenic contamination and mitigation #Metalloenzymes and iron-sulfur proteins #Nitrogen and Sulfur Effects on Brassica

paper · doi:10.1042/bst0340143

openalex publication_date 2006/01/20 · openalex created_date 2016/06/24 · openalex updated_date 2026/07/30

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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• Kinetic and thermodynamic resolution of the interactions between sulfite and the pentahaem cytochrome NrfA from Escherichia coli
• Substrate binding and activation in the active site of cytochrome c nitrite reductase: a density functional study

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