TY  - JOUR
AU  - Einsle, O.
AU  - Messerschmidt, A.
AU  - Stach, P.
AU  - Bourenkov, G. P.
AU  - Bartunik, H. D.
AU  - Huber, R.
AU  - Kroneck, P. M.
TI  - Structure of cytochrome c nitrite reductase
JO  - Nature 
VL  - 400
IS  - 6743
SN  - 0028-0836
CY  - London [u.a.]
PB  - Nature Publ. Group
M1  - PUBDB-2017-10855
SP  - 476 - 480
PY  - 1999
N1  - F-Bereich; Max-Planck-Gesellschaft
AB  - 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.
KW  - Cytochrome c Group (NLM Chemicals)
KW  - Nitrites (NLM Chemicals)
KW  - cytochrome c553 (NLM Chemicals)
KW  - Heme (NLM Chemicals)
KW  - cytochrome C-552 (NLM Chemicals)
KW  - Oxidoreductases (NLM Chemicals)
KW  - hydroxylamine dehydrogenase (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:10440380
UR  - <Go to ISI:>//WOS:000081715000057
DO  - DOI:10.1038/22802
UR  - https://bib-pubdb1.desy.de/record/392397
ER  -