Redox tuning of cytochrome b562 through facile metal porphyrin substitution

Chem Commun (Camb). 2012 Nov 7;48(86):10624-6. doi: 10.1039/c2cc34302a.

Abstract

The biologically and nanotechnologically important heme protein cytochrome b(562) was reconstructed with zinc and copper porphyrins, leading to significant changes in the spectral, redox and electron transfer properties. The Cu form shifts the redox potential by +300 mV and exhibits high electron transfer, while the Zn form is redox inert.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cytochrome b Group / chemistry*
  • Cytochrome b Group / metabolism
  • Electrochemical Techniques
  • Electron Transport
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / metabolism
  • Oxidation-Reduction
  • Protoporphyrins / chemistry*

Substances

  • Cytochrome b Group
  • Escherichia coli Proteins
  • Protoporphyrins
  • copper protoporphyrin IX
  • zinc protoporphyrin
  • cytochrome b562, E coli