Could CuB be the site of redox linkage in cytochrome c oxidase?

abstract

• This paper explores the proton pumping function of cytochrome c oxidase [ferrocytochrome-c:oxygen oxidoreductase (EC 1.9.3.1)] based upon redox linkage at the "high-potential" CuB center. A model is proposed that is derived from a redox-linked ligand exchange mechanism previously described for the CuA site. Qualitative analysis of this mechanism indicates that such a mechanism is feasible. However, the relatively short distance between CuB and cytochrome a3 implies that the uncoupling electron transfers are quite facile. In addition, the position of the CuB center with respect to the inner mitochondrial membrane argues against redox linkage at the CuB site.

authors

• Musser, Siegfried

published proceedings

• Proc Natl Acad Sci U S A

author list (cited authors)

• Larsen, R. W., Pan, L. P., Musser, S. M., Li, Z. Y., & Chan, S. I.

citation count

• 27

complete list of authors

• Larsen, RW||Pan, LP||Musser, SM||Li, ZY||Chan, SI

publication date

• January 1992

publisher

• Proceedings of the National Academy of Sciences  Publisher

published in

• Proceedings of the National Academy of Sciences of the United States of America  Journal

keywords

• Biological Transport, Active
• Copper
• Electron Transport
• Electron Transport Complex IV
• Hydrogen-Ion Concentration
• Intracellular Membranes
• Ligands
• Membrane Potentials
• Mitochondria
• Models, Biological
• Oxidation-Reduction

PubMed Central ID

• 1309955

Digital Object Identifier (DOI)

• 10.1073/pnas.89.2.723

start page

• 723

end page

• 727

volume

• 89

issue

• 2

URL

• http://dx.doi.org/10.1073/pnas.89.2.723