Pentahaem cytochrome c nitrite reductase: reaction with hydroxylamine, a 
potential reaction intermediate and substrate

Rudolf, M.; Einsle, O.; Neese, F.; Kroneck, P. M. H.

doi:10.1042/bst0300649

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Pentahaem cytochrome c nitrite reductase: reaction with hydroxylamine, a potential reaction intermediate and substrate

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Einsle, O.
Howard Hughes Medical Institute and Division of Chemistry and Chemical Engineering, California Institute of Technology;
Research Department Wieghardt, Max Planck Institute for Radiation Chemistry, Max Planck Society;

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Neese, F.
Howard Hughes Medical Institute and Division of Chemistry and Chemical Engineering, California Institute of Technology;
Research Department Wieghardt, Max Planck Institute for Radiation Chemistry, Max Planck Society;

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Citation

Rudolf, M., Einsle, O., Neese, F., & Kroneck, P. M. H. (2002). Pentahaem cytochrome c nitrite reductase: reaction with hydroxylamine, a potential reaction intermediate and substrate. Biochemical Society Transactions, 30(4), 649-653. doi:10.1042/bst0300649.

Cite as: https://hdl.handle.net/21.11116/0000-0007-F26E-D

Abstract

The pentahaem enzyme cytochrome c nitrite reductase catalyses the reduction of nitrite to ammonia, a key reaction in the biological nitrogen cycle. The enzyme can also transform nitrogen monoxide and hydroxylamine, two potential bound reaction intermediates, into ammonia. Structural and mechanistic aspects of the multihaem enzyme are discussed in comparison with hydroxylamine oxidoreductase, a trimeric protein with eight haem molecules per subunit.