A computational protocol to probe the role of solvation effects on the reduction potential of azurin mutants

Proteins. 2006 Jan 1;62(1):262-9. doi: 10.1002/prot.20772.

Abstract

Semiquantitative relationships between thermodynamic parameters of Cu2+ reduction experimentally measured for a series of azurin mutants and the solvation free energy of the oxidized state of the proteins were derived. Solvation free energy calculations were carried out within an ONIOM/PCM scheme specifically adapted to this protein series. The method proved to be able to capture the main determinants of the measured reduction parameters, providing satisfactory predictions of the E degrees '.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algorithms
  • Azurin / chemistry*
  • Azurin / genetics
  • Azurin / metabolism
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Enzymes / chemistry
  • Enzymes / metabolism
  • Mutation
  • Oxidation-Reduction
  • Solutions
  • Surface Properties

Substances

  • Bacterial Proteins
  • Enzymes
  • Solutions
  • Azurin