A combined quantum chemical and crystallographic study on the oxidized binuclear center of cytochrome c oxidase
Under an Elsevier user license
open archive
Research Highlights
► The oxidized active site of cytochrome c oxidase was studied by DFT. ► Results from DFT calculations were compared to X-ray diffraction data. ► Oxygenous species form a superoxide compound in the oxidized active site. ► Dianionic peroxide is expected to be cleaved in the oxidized active site. ► Dioxygen is consistent with the experimentally observed electron density.
Keywords
Heme-copper oxidases
Oxygen binding
Density functional theory (DFT)
X-ray refinement
Cited by (0)
- 1
Present address: Institut de Biologie Structurale (UMR 5075 CEA-CNRS-UJF), 46 rue Jules Horowitz, 38027 Grenoble Cedex 1, France.
Copyright © 2011 Elsevier B.V. All rights reserved.