Multifrequency EPR evidence for a bimetallic center at the CuA site in cytochrome c oxidase. FEBS Lett 1990 Jul 30;268(1):274-6
Date
07/30/1990Pubmed ID
2166686DOI
10.1016/0014-5793(90)81026-kScopus ID
2-s2.0-0025341616 (requires institutional sign-in at Scopus site) 140 CitationsAbstract
Multifrequency electron paramagnetic resonance (EPR) spectra of the Cu(II) site in bovine heart cytochrome c oxidase (COX) and nitrous oxide reductase (N2OR) from Pseudomonas stutzeri confirm the existence of Cu-Cu interaction in both enzymes. C-band (4.5 GHz) proves to be a particularly good frequency complementing the spectra of COX and N2OR recorded at 2.4 and 3.5 GHz. Both the high and low field region of the EPR spectra show the presence of a well-resolved 7-line pattern consistent with the idea of a binuclear Cu center in COX and N2OR. Based on this assumption consistent g-values are calculated for gz and gx at four frequencies. No consistent g-values are obtained with the assumption of a 4-line pattern indicative for a mononuclear Cu site.
Author List
Kroneck PM, Antholine WE, Kastrau DH, Buse G, Steffens GC, Zumft WGMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceAnimals
Binding Sites
Cattle
Copper
Electron Spin Resonance Spectroscopy
Electron Transport Complex IV
Molecular Sequence Data
Myocardium
Oxidoreductases
Pseudomonas
