Structural highlights
Function
O68601_ALCXX
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Copper nitrite reductases contain both an electron-transfer type 1 Cu site and a catalytic type 2 Cu site. We have mutated one of the type 2 copper ligating histidines to observe the effect on catalytic turnover. This mutation has created a unique site where Cu is ligated by 2 His Nepsilon2 atoms alone.
Observation of an unprecedented Cu Bis-His site: crystal structure of the H129V mutant of nitrite reductase.,Ellis MJ, Antonyuk SV, Strange RW, Sawers G, Eady RR, Hasnain SS Inorg Chem. 2004 Nov 29;43(24):7591-3. PMID:15554622[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ellis MJ, Antonyuk SV, Strange RW, Sawers G, Eady RR, Hasnain SS. Observation of an unprecedented Cu Bis-His site: crystal structure of the H129V mutant of nitrite reductase. Inorg Chem. 2004 Nov 29;43(24):7591-3. PMID:15554622 doi:10.1021/ic048966p
