The oxidation of cytochrome-c oxidase vesicles by hemoglobin. Biochim Biophys Acta 1994 Sep 21;1208(1):38-44
Date
09/21/1994Pubmed ID
8086437DOI
10.1016/0167-4838(94)90157-0Scopus ID
2-s2.0-0028112044 (requires institutional sign-in at Scopus site) 18 CitationsAbstract
Human hemoglobin has been used as a pro-oxidant for artificial unilamellar phospholipid vesicles, containing cytochrome-c oxidase inserted into the bilayer. This experimental system was suitable to follow directly the kinetics of lipid oxidation and the effects on both the vesicle membrane permeability and the functional state of cytochrome-c oxidase. Following mixing of vesicles with hemoglobin, an oxygen dependent, peroxyl radical mediated, rapid oxidation (taking a few minutes) of the lipid was found to occur. On a similar time scale the membrane became ion-leaky and cytochrome-c oxidase damaged. The pro-oxidant effects of hemoglobin in various oxidation and ligation states were studied and a mechanism, based on a ferric/ferryl redox cycle of the heme-iron is proposed to account for these observations.
Author List
Sarti P, Hogg N, Darley-Usmar VM, Sanna MT, Wilson MTAuthor
Neil Hogg PhD Senior Associate Dean, Professor in the Biophysics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Cell Membrane PermeabilityElectron Transport Complex IV
Hemoglobins
Humans
Kinetics
Lipid Bilayers
Lipid Peroxidation
Liposomes
Oxidation-Reduction
Oxygen Consumption
Peroxides
