期刊
FEBS LETTERS
卷 580, 期 5, 页码 1350-1354出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2006.01.055
关键词
FTIR; vibrational spectroscopy; cytochrome c; oxidase; respiration; proton translocation; electron transfer; glutamic acid; tyrosine; membrane; bacteriorhodopsin
Heme-copper oxygen reductases catalyze proton translocation across the cellular membrane; this takes place during the reaction of oxygen to water. We demonstrate with attenuated total reflection-Fourier transform infrared (ATR-FTIR) difference spectroscopy that a tyrosine residue of the oxygen reductase from the thermobalophilic Rhodothermus marinus becomes deprotonated in the transition from the oxidized state to the catalytic intermediate ferryl state Pm. This tyrosine residue is most probably Y256, the helix VI tyrosine residue proposed to substitute for the D-channel glutamic acid that is absent in this enzyme. Comparison with the mitochondrial like oxygen reductase from Rhodobacter sphaeroides suggests that proton transfer from a strategically situated donor to the active site is a crucial step in the reaction mechanism of oxygen reductases. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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