Please use this identifier to cite or link to this item:
Title: Discrete steps in dioxygen activation - the cytochrome oxidase/O2 reaction
Authors: Babcock, Gerald
Varotsis, Constantinos 
Keywords: Cytochrome oxidase;Hemoproteins;Oxygen;Electron transport;Oxidation-reduction reaction
Issue Date: 1993
Publisher: Springer
Source: Journal of bioenergetics and biomembranes, 1993, volume 25, issue 2, pages 71-80
Abstract: The kinetic constraints that are imposed on cytochrome oxidase in its dual function as the terminal oxidant in the respiratory process and as a redox- linked proton pump provide a unique opportunity to investigate the molecular details of biological O2 activation. By using flow/flash techniques, it is possible to visualize individual steps in the O2-binding and reduction process, and results from a number of spectroscopic investigations on the oxidation of reduced cytochrome oxidase by O2 are now available. In this article, we use these results to synthesize a reaction mechanism for O2 activation in the enzyme and to simulate time-concentration profiles for a number of intermediates that have been observed experimentally. Kinetic manifestation of the consequences of coupling exergonic electron transfer to endergonic proton translocation emerge from this analysis. Energetic efficiency in this process apparently requires that potentially toxic intermediate oxidation states of dioxygen accumulate to substantial concentration during the reduction reaction
ISSN: 0145-479X (print)
1573-6881 (online)
DOI: 10.1007/BF00762849
Rights: © 1993 Plenum Publishing Corporation
Type: Article
Appears in Collections:Άρθρα/Articles

Show full item record


checked on May 20, 2019

Citations 50

checked on Aug 13, 2019

Page view(s) 50

Last Week
Last month
checked on Aug 17, 2019

Google ScholarTM



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.