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Structure of cytochrome c nitrite reductase

Nature volume 400, pages 476–480 (1999)Cite this article

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.

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Figure 1: The nitrite reductase dimer.
Figure 2: Haem arrangement.
Figure 3: The active site of the enzyme.
Figure 4: The active-site channel.
Figure 5: Comparison between nitrite reductase (NiR) and hydroxylamine oxidoreductase (HAO).

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Acknowledgements

This work was supported by Volkswagenstiftung (P.K.), Deutsche Forschungsgemeinschaft (P.K.), Fonds der Chemischen Industrie (P.K.), EU-Biotech Project (O.E., A.M., R.H.) and the European Network MASIMO in Human Capital and Mobility (P.K., A.M.). We thank N. Pfennig and H.Beinert who initiated this research, and K. Sulger for assistance in the purification of nitrite reductase.

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Authors and Affiliations

  1. Abteilung Strukturforschung, Max-Planck-Institut für Biochemie, Am Klopferspitz 18a, Martinsried, 82152, Germany

    Oliver Einsle, Albrecht Messerschmidt & Robert Huber

  2. MPG-ASMB c/o DESY, Arbeitsgruppe Proteindynamik, Notkestrasse 85, 22603, Hamburg, Germany

    Gleb P. Bourenkov & Hans D. Bartunik

  3. Universität Konstanz, Fakultät für Biologie, Konstanz, 78457, Germany

    Oliver Einsle, Petra Stach & Peter M. H. Kroneck

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  1. Oliver Einsle
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Correspondence to Oliver Einsle.

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Einsle, O., Messerschmidt, A., Stach, P. et al. Structure of cytochrome c nitrite reductase. Nature 400, 476–480 (1999). https://doi.org/10.1038/22802

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