Structure of cytochrome c nitrite reductase

Oliver Einsle (), Albrecht Messerschmidt, Petra Stach, Gleb P. Bourenkov, Hans D. Bartunik, Robert Huber and Peter M. H. Kroneck
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Oliver Einsle: Max-Planck-Institut für Biochemie
Albrecht Messerschmidt: Max-Planck-Institut für Biochemie
Petra Stach: Universität Konstanz, Fakultät für Biologie
Gleb P. Bourenkov: MPG-ASMB c/o DESY, Arbeitsgruppe Proteindynamik
Hans D. Bartunik: MPG-ASMB c/o DESY, Arbeitsgruppe Proteindynamik
Robert Huber: Max-Planck-Institut für Biochemie
Peter M. H. Kroneck: Universität Konstanz, Fakultät für Biologie

Nature, 1999, vol. 400, issue 6743, 476-480

Abstract: Abstract The enzyme cytochrome c nitrite reductase catalyses the six-electron reduction of nitrite to ammonia as one of the key stepsin the biological nitrogen cycle1, where it participates inthe anaerobic energy metabolism of dissimilatory nitrate ammonification2. Here we report on the crystal structure of this enzyme from the microorganism Sulfurospirillum deleyianum, which we solved by multiwavelength anomalous dispersion methods. We propose a reaction scheme for the transformation of nitrite based on structural and spectroscopic information. Cytochrome c nitrite reductase is a functional dimer, with 10 close-packed haem groups of type c and an unusual lysine-coordinated high-spin haem at the active site. By comparing the haem arrangement of this nitrite reductase with that of other multihaem cytochromes, we have been able to identify a family of proteins in which the orientation of haem groups is conserved whereas structure and function are not.

Date: 1999
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DOI: 10.1038/22802

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