Involvement of a Glu71-Arg64 couple in the access channel for NADH in cytochrome p450nor.
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.
Su
Fei
F
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
Fushinobu
Shinya
S
Takaya
Naoki
N
Shoun
Hirofumi
H
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
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)