Please use this identifier to cite or link to this item: http://ktisis.cut.ac.cy/handle/10488/6611
Title: Ligand binding in a docking site of cytochrome c oxidase: a time-resolved step-scan fourier transform infrared study
Authors: Soulimane, Tewfik 
Varotsis, Constantinos 
Koutsoupakis, Constantinos 
Keywords: Enzymes
Catalysis
Fourier transform infrared spectroscopy
Ligand binding (Biochemistry)
Carbon monoxide
Cytochrome oxidase
Heme
Dissociation
Issue Date: 2003
Publisher: ACS Publications
Source: Journal of the american chemical society, 2003, volume 125, issue 48, pages 14728-14732
Abstract: The description of reaction regulation in enzymes responsible for activating and catalyzing small molecules (O2, NO) requires identification of ligand movement into the binding site and out of the enzyme through specific channels and docking sites. We have used time-resolved step-scan Fourier transform infrared spectroscopy on CO-photolyzed cytochrome c oxidase ba3 from T. thermophilus, which is responsible for the activation and reduction of both O2 and NO, to gain insight into the structure of ligand-binding intermediates at ambient temperature. We show that, upon dissociation, the photolyzed CO becomes trapped within a ligand docking site located near the ring A proplonate of heme a3. The 2131 cm -1 mode of the "docked" CO we have detected corresponds to the B1 state of Mb and persists for 35 μs. The release of CO from the docking site is not followed by recombination to the heme a3 Fe. Our analysis indicates that this behavior reflects a mechanism in which the protein near ring A of heme a3propionate reorganizes about the released CO from the docking site, and establishes a transient barrier that inhibits the recombination process to the heme a3 Fe for a few milliseconds. Rebinding to heme a3 occurs with k2 = 29.5 s-1. These results have implications for understanding the role of ligand binding/escape through docking sites and channels in heme-copper oxidases and, thus, in respiration
URI: http://ktisis.cut.ac.cy/handle/10488/6611
ISSN: 00027863
DOI: 10.1021/ja036107e
Rights: Copyright © 2003 American Chemical Society
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