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Resonance Raman spectroscopic study of the caa(3) oxidase from Thermus thermophilus
Citation key ISI:000077234300002
Author Gerscher, S and Hildebrandt, P and Soulimane, T and Buse, G
Pages 365-377
Year 1998
ISSN 1075-4261
Address BAFFINS LANE CHICHESTER, W SUSSEX PO19 1UD, ENGLAND
Journal Biospectroscopy
Volume 4
Number 6
Publisher JOHN WILEY & SONS LTD
Abstract The terminal caa(3) oxidase of Thermus thermophilus has been studied by resonance Raman spectroscopy. Using different excitation wavelengths in the Soret band region, it was possible to disentangle the resonance Raman spectra of the fully oxidized and fully reduced state in terms of the component spectra of the individual hemes a, a(3), and c. For the heme a and a(3) groups, the spectra reveal only minor differences compared to those of beef heart cytochrome c oxidase attributable to subtle modifications of the heme environment. These differences are not more pronounced than those between the oxidases from beef heart and Paracoccus dentitrificans confirming the view that this oxidase of Th. thermophilus is a typical member of the aa(3) oxidase superfamily. The heme c component spectra display far-reaching similarities with those of c-type cytochromes which serve as mobile electron carriers in the respiratory chain. These results imply that caa(3) oxidase represents an integrated version of the noncovalent redox complex between cytochrome c and cytochrome c oxidase in higher organisms. On the other hand, the structural changes of cytochrome c in the noncovalent complex have no counterpart in the heme c component of the caa(3) oxidase indicating a specific cytochrome c binding site for the mitochondrial enzyme. (C) 1998 John Wiley & Sons, Inc.
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