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ATR-FTIR Spectroscopy of the PM and F Intermediates of Bovine and Paracoccus denitrificans Cytochrome c Oxidase



ATR-FTIR Spectroscopy of the PM and F Intermediates of Bovine and Paracoccus denitrificans Cytochrome c Oxidase



Biochemistry (American Chemical Society) 42(29): 09-17



The structures of PM and F intermediates of bovine and Paracoccus denitrificans cytochrome c oxidase were investigated by perfusion-induced attenuated total reflection-Fourier transform infrared (ATR-FTIR) spectroscopy. Transitions from the "fast" oxidized state to the PM) or F states were initiated by perfusion with buffer containing either CO/oxygen or H2O2. Intermediates were quantitated by simultaneous monitoring of visible absorption changes in the protein film. For both bovine and P. denitrificans oxidase, the major features of the IR difference spectrum of PM were similar when produced by CO/oxygen or by H2O2 treatments. These IR difference spectra were distinctly different from the IR difference spectrum of F that formed with extended treatment with H2O2. Some IR bands could be assigned tentatively to perturbations of heme a3 ring modes and substituents, and these perturbations were greater in PM than in F. Other bands could be assigned to surrounding protein changes. Strong perturbation of the environment of a carboxylic acid, most likely E-242 (bovine numbering), occurred in PM and relaxed back in F. A second redox-sensitive carboxylic acid was also perturbed in the bovine PM intermediate. Further consistent signatures of PM in both oxidases that were absent in F were strong negative bands at 1547 and 1313 cm-1 in bovine oxidase (1542 and 1314 cm-1 in P. denitrificans) and a positive band at approximately 1519 cm-1. From comparison with available IR data on model compounds, it is suggested that these reflect changes in the covalent tyrosine-histidine ligand to CuB. These findings are discussed in relation to the oxidase catalytic cycle. Reprinted by permission of the publisher.

Accession: 009758109

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PMID: 12873142

DOI: 10.1021/bi034522d

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