Please use this identifier to cite or link to this item: https://ktisis.cut.ac.cy/handle/10488/11062
Title: Ligand Dynamics in the Binuclear Site in Cytochrome Oxidase
Authors: Babcock, Gerald 
Deinum, Geurt 
Hosler, Jon 
Younkyoo, Kim 
Pressler, Michelle 
Proshlyakov, Denis A. 
Schelvis, Hans 
Varotsis, Constantinos 
Ferguson-Miller, Shelagh 
Keywords: Oxygen activation;Proton pum;Ligand shuttle;Ligand photolysis;Respiration
Category: Chemical Sciences
Field: Natural Sciences
Issue Date: 1998
Publisher: Springer-Verlag Tokyo
Source: Oxygen Homeostasis and Its Dynamics, 1998, Pages 47-56
DOI: https://doi.org/10.1007/978-4-431-68476-3_6
Abstract: The dioxygen-reduction mechanism in cytochrome oxidase relies on proton control of the electron-transfer events that drive the process. Recent work on proton delivery and efflux channels in the protein that are relevant to substrate reduction and proton pumping is considered, and the current status of this area is summarized. Carbon monoxide photo dissociation and the ligand dynamics that occur subsequent to photolysis have been valuable tools in probing possible coupling schemes for linking exergonic electron-transfer chemistry to endergonic proton translocation. Our picosecond-time-resolved Raman results show that the heme a3- proximal histidine bond remains intact following CO photo dissociation but that the local environment around the heme a3 center in the photoproduct is in a nonequilibrium state. This photoproduct relaxes to its equilibrium configuration on the same time scale as ligand release occurs from CUB' which suggests a coupling between the two events and a potential signaling pathway between the site of O2 binding and reduction and the putative element, CUB' that links the redox chemistry to the proton pump.
URI: http://ktisis.cut.ac.cy/handle/10488/11062
ISBN: 978-4-431-68476-3
Rights: © Springer-Verlag Tokyo 1998
Type: Book Chapter
Appears in Collections:Κεφάλαια βιβλίων/Book chapters

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