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The methanol cytochrome c oxido reductase activity of methylotrophs

Journal of General Microbiology 129(4): 923-934

The methanol cytochrome c oxido reductase activity of methylotrophs

The soluble cytochromes c of the obligate methylotroph, Methylophilus methylotrophus, were rapidly autoreducible at high pH. The intramolecular autoreduction mechanism was also involved in the reduction of the cytochrome cL by methanol dehydrogenase which occurred in the absence of methanol. Pure soluble methanol dehydrogenase catalyzes the methanol-dependent reduction of pure cytochrome c from M. methylotrophus and from the facultative methylotroph Pseudomonas AM1 by coupling oxidation of the bacterial cytochrome to the reduction of a large excess of mammalian cytochrome c. Only 1 of the 2 cytochromes c (cytochrome cL of each organism) could react with methanol dehydrogenase to give methanol:cytochrome c oxidoreductase activity. This activity, using proteins from M. methylotrophus, was independent of pH between 7.0-9.0 and ammonia was not required. The pH optimum for the system from Pseudomonas AM1 was 9.0 and activity was stimulated .apprx. 4-fold by NH4Cl. The product of methanol oxidation was formaldehyde, which was also a substrate for the oxidoreductase system. During formaldehyde oxidation 2 molecules of cytochrome c were reduced for every molecule of formaldehyde oxidized. In a survey of methanol dehydrogenases and cytochromes c from Pseudomonas AM1, M. methylotrophus and the facultative autotroph, Paracoccus denitrificans, it was shown that, of the two soluble cytochromes c found in each methylotroph, only one was able to react with methanol dehydrogenase. The cytochrome cL from M. methylotrophus and the cytochrome c(2) of P. denitrificans were specific, only reacting with methanol dehydrogenase from the same organism, whereas the cytochrome cL of Pseudomonas AM1 reacted with all 3 methanol dehydrogenases tested.

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Accession: 006717929

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