Interheme electron tunneling in cytochrome c oxidase

• Published in: Proceedings of the National Academy of Sciences - PNAS 2010-12, Vol.107 (50), p.21470-21475
• Main Authors: Kaila, Ville R. I., Johansson, Mikael P., Sundholm, Dage, Wikström, Mårten, Gray, Harry B.
• Format: Article
• Language: English
• Subjects: Atoms; Bacteria; Binding sites; Biological Sciences; Copper - chemistry; Cytochromes; Electron transfer; Electron Transport; Electron Transport Complex IV - chemistry; Electron tunneling; Electrons; Energy; Enzymes; Eukaryotes; Heme - chemistry; Models, Molecular; Molecular Dynamics Simulation; Molecules; Oxidases; Oxidation-Reduction; Oxygen; Oxygen - chemistry; Packing density; Protein Conformation; Protons; Quantum Theory
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.1005889107

Cytochrome c oxidase (CcO) is the terminal enzyme of the respiratory chain that catalyzes respiratory reduction of dioxygen (O₂) to water in all eukaryotes and many aerobic bacteria. CcO, and its homologs among the heme-copper oxidases, has an active site composed of an oxygen-binding heme and a copper center in the vicinity, plus another heme group that donates electrons to this site. In most oxidoreduction enzymes, electron transfer (eT) takes place by quantum-mechanical electron tunneling. Here we show by independent molecular dynamics and quantum-chemical methods that the heme-heme eT in CcO differs from the majority of cases in having an exceptionally low reorganization energy. We show that the rate of interheme eT in CcO may nevertheless be predicted by the Moser-Dutton equation if reinterpreted as the average of the eT rates between all individual atoms of the donor and acceptor weighed by the respective packing densities between them. We argue that this modification may be necessary at short donor/acceptor distances comparable to the donor/acceptor radii.