Membrane environment drives cytochrome P450's spin transition and its interaction with cytochrome b5

Chem Commun (Camb). 2017 Nov 28;53(95):12798-12801. doi: 10.1039/c7cc07520k.

Abstract

Heme's spin-multiplicity is key in determining the enzymatic function of cytochrome P450 (cytP450). The origin of the low-spin state in ferric P450 is still under debate. Here, we report the first experimental demonstration of P450's membrane interaction altering its spin equilibrium which is accompanied by a stronger affinity for cytochrome b5. These results highlight the importance of lipid membrane for the function of P450.

MeSH terms

  • Cytochrome P-450 Enzyme System / chemistry
  • Cytochrome P-450 Enzyme System / metabolism*
  • Cytochromes b5 / chemistry
  • Cytochromes b5 / metabolism*
  • Models, Molecular

Substances

  • Cytochromes b5
  • Cytochrome P-450 Enzyme System