Observation of an unprecedented Cu Bis-His site: crystal structure of the H129V mutant of nitrite reductase.
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.
Ellis
Mark J
MJ
Molecular Biophysics Group, CCLRC Daresbury Laboratory, Warrington, Cheshire, UK.
Antonyuk
Svetlana V
SV
Strange
Richard W
RW
Sawers
Gary
G
Eady
Robert R
RR
Hasnain
S Samar
SS
D019943:Amino Acid Substitution; D020134:Catalytic Domain; D003300:Copper / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D004578:Electron Spin Resonance Spectroscopy; D006639:Histidine / Q000737:chemistry* / Q000378:metabolism; D008024:Ligands; D008958:Models, Molecular; D009154:Mutation / Q000235:genetics*; D009572:Nitrite Reductases / Q000737:chemistry* / Q000378:metabolism; D009942:Organometallic Compounds / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D008024:Ligands; D009942:Organometallic Compounds; D006639:Histidine; D003300:Copper; D009572:Nitrite Reductases; C052695:nitrite reductase, copper-containing