SUMMARY: Cytochromes of the and types in membranes from the thermophilic bacterium PS3 have been characterized with respect to their spectral, potentiometric and ligand-binding properties. The integrated approach used (a) conventional potentiometric analysis with non-linear least-square analysis, (b) incorporation of the potentiometric procedures into a spectral decomposition protocol at 298 and 77 K, (c) fourth-order finite difference and fourth derivative analysis, and (d) photodissociation studies of the CO-liganded components. Either one -type cytochrome with a split α-band (547, 552 nm at 77 K) or two cytochromes with similar redox potentials lapprox. +230 mV) were found, together with at least three -type cytochromes (554, 557 and 561 nm at 77 K). On the basis of its high redox potential (+104mV), cytochrome was tentatively equated with the -type oxidase of this organism. A c-type cytochrome that formed a photodissociable complex with CO was also detected. The α-band of the previously purified cytochrome oxidase was resolved into two components, having spectral and potentiometric properties remarkably similar to those of the analogous mitochondrial oxidase.


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