Structure of cytochrome P450 2B4 with an acetate ligand and an active site hydrogen bond network similar to oxyferrous P450cam

J Inorg Biochem. 2018 Aug:185:17-25. doi: 10.1016/j.jinorgbio.2018.04.015. Epub 2018 Apr 30.

Abstract

Superposition of the active site of acetate-bound P4502B4 and oxyferrous P450cam. Bond lengths between the heme iron, the sixth ligand, and the hydroxyl of the conserved threonine are shown. Note that different threonine rotamers form the hydrogen bonds to the acetate and oxygen.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Acetates / chemistry*
  • Animals
  • Aryl Hydrocarbon Hydroxylases / chemistry*
  • Catalytic Domain
  • Crystallography, X-Ray
  • Cytochrome P450 Family 2 / chemistry
  • Ferrous Compounds / chemistry
  • Glutamic Acid / chemistry
  • Hydrogen Bonding
  • Ligands
  • Oxygen / chemistry
  • Protein Conformation
  • Rabbits
  • Static Electricity

Substances

  • Acetates
  • Ferrous Compounds
  • Ligands
  • Glutamic Acid
  • Aryl Hydrocarbon Hydroxylases
  • Cytochrome P450 Family 2
  • cytochrome P-450 CYP2B4 (rabbit)
  • Oxygen