Involvement of a Glu71-Arg64 couple in the access channel for NADH in cytochrome p450nor

Biosci Biotechnol Biochem. 2004 May;68(5):1156-9. doi: 10.1271/bbb.68.1156.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution / genetics
  • Arginine / chemistry
  • Aspartic Acid / chemistry
  • Cytochrome P-450 Enzyme System / chemistry*
  • Cytochrome P-450 Enzyme System / genetics*
  • Fusarium / enzymology
  • Glutamic Acid / chemistry
  • Heme / chemistry
  • Molecular Structure
  • NAD / chemistry*
  • Oxidoreductases / chemistry*
  • Oxidoreductases / genetics*
  • Point Mutation

Substances

  • NAD
  • Aspartic Acid
  • Glutamic Acid
  • Heme
  • Cytochrome P-450 Enzyme System
  • Arginine
  • Oxidoreductases
  • nitric-oxide reductase (P450)