Spectroscopic and Kinetic Investigation of the Fully Reduced and Mixed Valence States of Ba 3-Cytochrome C Oxidase From Hermus Thermophilus a Fourier Transform Infrared (FTIR) and Time-Resolved Step-Scan FTIR Study

Please use this identifier to cite or link to this item: https://hdl.handle.net/20.500.14279/3300

Title:	Spectroscopic and Kinetic Investigation of the Fully Reduced and Mixed Valence States of Ba 3-Cytochrome C Oxidase From Hermus Thermophilus a Fourier Transform Infrared (FTIR) and Time-Resolved Step-Scan FTIR Study
Authors:	Koutsoupakis, Constantinos Soulimane, Tewfik Varotsis, Constantinos
Major Field of Science:	Natural Sciences
Field Category:	Chemical Sciences
Keywords:	Porphyrins;Photochemistry;Cytochrome oxidase;Carbon monoxide;Infrared spectroscopy;Thermodynamics
Issue Date:	27-Aug-2012
Source:	Journal of Biological Chemistry, vol. 287, no. 44, pp. 37495-37507
Volume:	287
Issue:	44
Start page:	37495
End page:	37507
Journal:	Journal of Biological Chemistry
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:	https://hdl.handle.net/20.500.14279/3300
ISSN:	1083351X
DOI:	10.1074/jbc.M112.403600
Rights:	© 2012 by The American society for biochemistry and molecular biology, Inc
Type:	Article
Affiliation :	Cyprus University of Technology University of Limerick
Appears in Collections:	Άρθρα/Articles

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