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The role of the conserved tryptophan272 of the Paracoccus denitrificans cytochrome c oxidase in proton pumping



The role of the conserved tryptophan272 of the Paracoccus denitrificans cytochrome c oxidase in proton pumping



Biochimica et Biophysica Acta 1777(7-8): 925-928



The catalytic mechanism of heme-copper oxidases - electron transfer coupled to proton pumping - is not yet fully understood. Single turnover experiments in which fully reduced cytochrome aa(3) from Paracoccus denitrificans reacts with O(2) using the microsecond freeze-hyperquenching sampling technique enabled trapping of transient catalytic intermediates and analysis by low temperature UV-Visible, X-band and Q-band EPR spectroscopy. Our recent findings (Wiertz et al. (2007) J. Biol. Chem. 282, 31580-31591), which show that the strictly conserved W272 is a redox active residue are reviewed here. The W272 forms a tryptophan neutral radical in the transition F-->F(W)-->O(H) in which the novel intermediate F(W) harbors the tryptophan radical. The potential role of W272 in proton pumping is highlighted.

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Accession: 056487367

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PMID: 18515062

DOI: 10.1016/j.bbabio.2008.05.008



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