Spectral and catalytic properties of cytochrome oxidase in organic solvents.
Isolated bovine heart cytochrome oxidase has been extracted into n-hexane, probably in reverse micelles, by the use of asolectin and calcium. The diluted extracts are composed of particles with the hydrodynamic radius of 42 nm. Spectral characteristics of the extracted oxidase are similar to those in aqueous solutions. At the high molar ratio of water to phospholipid (W0 = 8) in an organic solvent both cytochrome a and a3 are reducible and oxygen uptake is observed. However, at low W0 (W0 = 1.8) the rate of cytochrome a reduction is decreased and reduction of cytochrome a3 is inhibited.
Bona
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Institute of Experimental Physics, Slovak Academy of Sciences, Kosice, Czechoslovakia.
Fabian
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Sedlák
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D000818:Animals; D002417:Cattle; D003576:Electron Transport Complex IV / Q000378:metabolism*; D007700:Kinetics; D008027:Light; D008929:Mitochondria, Heart / Q000201:enzymology; D010084:Oxidation-Reduction; D010101:Oxygen Consumption; D011048:Polarography; D012542:Scattering, Radiation; D012997:Solvents; D013053:Spectrophotometry
D012997:Solvents; D003576:Electron Transport Complex IV