A random-sequential mechanism for nitrite binding and active site reduction in copper-containing nitrite reductase.

Journal article

The homotrimeric copper-containing nitrite reductase (NiR) contains one type-1 and one type-2 copper center per monomer. Electrons enter through the type-1 site and are shuttled to the type-2 site where nitrite is reduced to nitric oxide. To investigate the catalytic mechanism of NiR the effects of pH and nitrite on the turnover rate in the presence of three different electron donors at saturating concentrations were measured. The activity of NiR was also measured electrochemically by exploit...

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Authors: Wijma, H; Jeuken, L; Verbeet, M; Armstrong, F; Canters, G

• Publication status: Published
• Journal: Journal of biological chemistry
• Volume: 281
• Issue: 24
• Pages: 16340-16346
• Publication date: 2006-06-01
• DOI: 10.1074/jbc.m601610200
• EISSN: 1083-351X
• ISSN: 0021-9258
• Language: English
• Keywords: Binding Sites; Electrochemistry; Nitrites; Hydrogen-Ion Concentration; Catalytic Domain; Protein Binding; Nitrite Reductases; Kinetics; Electrons; Models, Chemical; Biochemistry; Alcaligenes faecalis