1QDB

CYTOCHROME C NITRITE REDUCTASE

Summary for 1QDB

• Entry DOI: 10.2210/pdb1qdb/pdb
• Descriptor: CYTOCHROME C NITRITE REDUCTASE, CALCIUM ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: c-type cytochrome lysine-coordinated heme nitrite reductase, oxidoreductase
• Biological source: Sulfurospirillum deleyianum
• Cellular location: Periplasm: Q9Z4P4
• Total number of polymer chains: 3
• Total formula weight: 170391.39

Authors

Einsle, O.,Messerschmidt, A.,Stach, P.,Huber, R.,Kroneck, P.M.H. (deposition date: 1999-05-19, release date: 1999-08-18, Last modification date: 2024-11-20)

Primary citation

Einsle, O.,Messerschmidt, A.,Stach, P.,Bourenkov, G.P.,Bartunik, H.D.,Huber, R.,Kroneck, P.M.
Structure of cytochrome c nitrite reductase.
Nature, 400:476-480, 1999

PubMed Abstract: The enzyme cytochrome c nitrite reductase catalyses the six-electron reduction of nitrite to ammonia as one of the key steps in the biological nitrogen cycle, where it participates in the anaerobic energy metabolism of dissimilatory nitrate ammonification. 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.

PubMed: 10440380
DOI: 10.1038/22802

Experimental method

X-RAY DIFFRACTION (1.9 Å)