A comparative EPR investigation of the multicopper proteins nitrous-oxide reductase and cytochrome c oxidase.
The multicopper proteins, nitrous-oxide reductase (N2OR) and cytochrome c oxidase (COX), were investigated by EPR spectroscopy at microwave frequencies 2.4-35 GHz. Our results support a Cu-Cu interaction in COX and N2OR. At least 10 lines in the 2.7-GHz, 12 lines in the 4.6-GHz and 14 lines in the 9.2 GHz spectra were resolved for N2OR. Eight copper lines at 2.7 GHz, about nine lines at 4.6 GHz and about six lines at 9.2 GHz were resolved for COX. Simulations of the EPR spectra were consistent with most of the resonances of the multiline spectra, including regions in the center of the spectra where overlap of the three seven-line patterns is proposed. These simulations indicated that Cu-Cu interaction, in a mixed-valence [Cu(1.5) ... Cu(1.5)], S = 1/2 site is consistent with, if not proof of, the unusual spectral features observed for N2OR and COX.
Antholine
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National Biomedical ESR Center, Medical College of Wisconsin, Milwaukee.
Kastrau
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Steffens
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Buse
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Zumft
W G
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Kroneck
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PM
D000818:Animals; D002417:Cattle; D003300:Copper / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D003576:Electron Transport Complex IV / Q000737:chemistry*; D009206:Myocardium / Q000201:enzymology; D010088:Oxidoreductases / Q000737:chemistry*; D010231:Paracoccus denitrificans / Q000201:enzymology; D011549:Pseudomonas / Q000201:enzymology
D003300:Copper; D010088:Oxidoreductases; C022763:nitrous oxide reductase; D003576:Electron Transport Complex IV