Journal Article

PUBDB-2017-10855

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structure of cytochrome c nitrite reductase

Einsle, O. (Corresponding author)Extern* ; Messerschmidt, A. ; Stach, P. ; Bourenkov, G. P. ; Bartunik, H. D. ; Huber, R. ; Kroneck, P. M.

1999
Nature Publ. Group London [u.a.]

This record in other databases:        

Please use a persistent id in citations: doi:10.1038/22802

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.

Keyword(s): Cytochrome c Group ; Nitrites ; cytochrome c553 ; Heme ; cytochrome C-552 ; Oxidoreductases ; hydroxylamine dehydrogenase

Note: F-Bereich; Max-Planck-Gesellschaft

---

Contributing Institute(s):

1. DESY Retrocat (DESY(-2012))

Research Program(s):

1. 899 - ohne Topic (POF3-899) (POF3-899)

Experiment(s):

1. No specific instrument

---

Database coverage:
; BIOSIS Previews ; Current Contents - Agriculture, Biology and Environmental Sciences ; Current Contents - Life Sciences ; Current Contents - Physical, Chemical and Earth Sciences ; Ebsco Academic Search ; IF >= 30 ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection ; Zoological Record

---