Please use this identifier to cite or link to this item: http://ktisis.cut.ac.cy/handle/10488/6557
Title: Spectroscopic and kinetic investigation of the fully reduced and mixed valence states of ba 3-cytochrome c oxidase from thermus thermophilus a fourier transform infrared (FTIR) and time-resolved step-scan FTIR study
Authors: Koutoupakis, Constantinos 
Soulimane, Tewfik 
Varotsis, Constantinos 
Keywords: Porphyrins;Photochemistry;Cytochrome oxidase;Carbon monoxide;Infrared spectroscopy;Thermodynamics
Category: Chemical Sciences
Field: Natural Sciences
Issue Date: 2012
Publisher: The American society for biochemistry and molecular biology
Source: Journal of biological chemistry, Volume 287, Issue 44, Pages 37495-37507
Abstract: Background: Cytochrome c oxidase reduces O 2 to H 2O, a reaction coupled to proton translocation across the membrane. Results: Photolysis of CO from the mixed valence form of cytochrome ba 3-CO does not lead to a heme a 3 3+-Cu B 1+-CO binuclear center. Conclusion: The absence of reverse electron transfer between hemes a 3 and b is shown. Significance: Unique thermodynamic and kinetic properties of cytochrome ba 3 oxidase are presented
URI: http://ktisis.cut.ac.cy/handle/10488/6557
ISSN: 00219258
DOI: 10.1074/jbc.M112.403600
Rights: © 2012 by The American society for biochemistry and molecular biology, Inc
Type: Article
Appears in Collections:Άρθρα/Articles

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