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.
journal_name
Naturejournal_title
Natureauthors
Einsle O,Messerschmidt A,Stach P,Bourenkov GP,Bartunik HD,Huber R,Kroneck PMdoi
10.1038/22802keywords:
subject
Has Abstractpub_date
1999-07-29 00:00:00pages
476-80issue
6743eissn
0028-0836issn
1476-4687journal_volume
400pub_type
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