Abstract
Membrane preparations from Synechococcus 6301 and 6311 exhibited low-temperature electron paramagnetic resonance (EPR) spectra in the g = 2.08 region characteristic of copper. The physical parameters of the power-saturation characteristics and the temperature-dependence profile demonstrated that the copper signals arose from a center in an environment identical to the aa 3 -type cytochrome- c oxidases reported in mammalian, yeast, and bacterial systems. Membrane purification procedures demonstrated that the oxidase was present in the cytoplasmic membrane at 10 times the level present in the thylakoid membrane. The copper was demonstrated to be fully redox active by its reducibility with physiological electron donors.
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