title: Observation of an unprecedented Cu Bis-His site: crystal structure of the H129V mutant of nitrite reductase.
abstract: 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.
authors.affiliation: Molecular Biophysics Group, CCLRC Daresbury Laboratory, Warrington, Cheshire, UK.
authors.forename: Mark J
authors.initials: MJ
authors.lastname: Ellis
authors.forename: Svetlana V
authors.initials: SV
authors.lastname: Antonyuk
authors.forename: Richard W
authors.initials: RW
authors.lastname: Strange
authors.forename: Gary
authors.initials: G
authors.lastname: Sawers
authors.forename: Robert R
authors.initials: RR
authors.lastname: Eady
authors.forename: S Samar
authors.initials: SS
authors.lastname: Hasnain
mesh_terms: 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
chemical_list: D008024:Ligands; D009942:Organometallic Compounds; D006639:Histidine; D003300:Copper; D009572:Nitrite Reductases; C052695:nitrite reductase, copper-containing