Redox potential of the cytochrome c in the flavocytochrome p‐cresol methylhydroxylase

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Abstract
The redox potential of the cytochrome c in 5 flavocytochrome c proteins, all p‐cresol methylhydroxylases purified from species of Pseudomonas, was measured. All gave similar values ranging from 226–250 mV. Two of the enzymes, from Pseudomonas putida NC1B 9866 and NC1B 9869, were resolved into their flavoprotein and cytochrome subunits and the redox potentials of the isolated cytochrome c subunits measured. The values for these were 60–70 mV below those for the whole enzymes but, in both cases, reconstitution of active enzyme by addition of the flavoprotein subunit restored the original potential.