Molecular dynamics calculations on peroxidases: the effect of calcium ions on protein structure

  • L. Banci
  • Paolo Carloni
  • Antonio Diaz
  • Giovanni Gori Savellini
ORIGINAL ARTICLE

DOI: 10.1007/s007750050052

Cite this article as:
Banci, L., Carloni, P., Diaz, A. et al. JBIC (1996) 1: 264. doi:10.1007/s007750050052

Abstract

 Molecular dynamics (MD) calculations were performed on two peroxidases, lignin peroxidase (LiP) and horseradish peroxidase (HRP), in the presence of the two endogenous calcium ions. The resulting averaged structures were compared to the structures obtained in the absence of the calcium ions. The overall protein folding was not affected by the presence or the lack of the calcium ions, while the active site was perturbed. In particular, on the distal side, a sizeable rearrangement of the distal histidine was observed in the absence of the calcium ions. These structural rearrangements are critically discussed with respect to the enzymatic mechanism.

Key words Molecular dynamicsPeroxidaseCalcium ionsStructure

Copyright information

© Society of Biological Inorganic Chemistry 1996

Authors and Affiliations

  • L. Banci
    • 1
  • Paolo Carloni
    • 1
  • Antonio Diaz
    • 1
  • Giovanni Gori Savellini
    • 1
  1. 1.Department of Chemistry, University of Florence, Via Gino Capponi 7, I-50121 Florence, ItalyIT