A near-infrared investigation of cytochrome c oxidase in higher plant mitochondria.
Optical features of cytochrome c oxidase in potato mitochondria have been characterized in the near-ir region. In order to discriminate the respective properties of the various redox centers, the redox state was monitored from free and inhibited, bound species. Appropriate comparisons singled out difference spectra which can be attributed specifically to CuA and CuB. The CuA difference spectrum (red-ox) exhibits a negative band centered at 812 nm and, analogous to its mammalian counterpart, the so-called 830-nm band (delta epsilon red/ox = -2.0 mM-1 cm-1). The unusual difference spectrum (red-ox) assigned to CuB is characterized by a broad positive band also centered at 812 nm with an extinction coefficient of delta epsilon red/ox = 4.3 mM-1 cm-1.
D001665:Binding Sites; D003300:Copper / Q000302:isolation & purification; D003486:Cyanides / Q000378:metabolism; D003576:Electron Transport Complex IV / Q000302:isolation & purification*; D008928:Mitochondria / Q000201:enzymology; D010084:Oxidation-Reduction; D010944:Plants / Q000201:enzymology*; D013055:Spectrophotometry, Infrared
D003486:Cyanides; D003300:Copper; D003576:Electron Transport Complex IV