title: Involvement of a Glu71-Arg64 couple in the access channel for NADH in cytochrome p450nor.
abstract: Putative access channel for NADH in the heme-distal pocket of cytochrome p450nor (p450nor) comprises many charged amino acid residues. Characterization of the E71A mutant protein of p450nor highlights the existence of a unique mechanism for binding NADH that depends on the salt bridge network between Glu71, Arg64 and Asp88.
authors.affiliation: Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
authors.forename: Fei
authors.initials: F
authors.lastname: Su
authors.forename: Shinya
authors.initials: S
authors.lastname: Fushinobu
authors.forename: Naoki
authors.initials: N
authors.lastname: Takaya
authors.forename: Hirofumi
authors.initials: H
authors.lastname: Shoun
mesh_terms: D019943:Amino Acid Substitution / Q000235:genetics; D001120:Arginine / Q000737:chemistry; D001224:Aspartic Acid / Q000737:chemistry; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000235:genetics*; D005670:Fusarium / Q000201:enzymology; D018698:Glutamic Acid / Q000737:chemistry; D006418:Heme / Q000737:chemistry; D015394:Molecular Structure; D009243:NAD / Q000737:chemistry*; D010088:Oxidoreductases / Q000737:chemistry* / Q000235:genetics*; D017354:Point Mutation
chemical_list: D009243:NAD; D001224:Aspartic Acid; D018698:Glutamic Acid; D006418:Heme; D003577:Cytochrome P-450 Enzyme System; D001120:Arginine; D010088:Oxidoreductases; C080610:nitric-oxide reductase (P450)