Ligand Dynamics in the Binuclear Site in Cytochrome Oxidase
Date Issued
1998
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.
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.