Add time:08/29/2019         Source:sciencedirect.com

Publisher SummaryThis chapter discusses the biochemical and physiological functions of pyrroloquinoline quinone (PQQ). Quinoproteins are distributed widely among prokaryotic and eukaryotic organisms. The prosthetic group of copper-containing amine oxidases from mammals, plants, and microorganisms have been identified as PQQ bound covalently to the enzyme protein. There has been controversy over a long period about the entity of the prosthetic group of the enzyme. The coupling of methylamine dehydrogenase to the respiratory chain is clearer than the coupling of methanol dehydrogenase to the respiratory chain. There is, however, still some controversy as to the natural electron acceptor for methylamine dehydrogenase and mechanisms of structural interaction between the dehydrogenase and a blue copper protein, amicyanin. Although there is a general agreement that amicyanin is the physiological electron acceptor for methylamine dehydrogenase, it is not necessarily detected in all methylotrophs grown on methylamine. In any event, because terminal oxidase is embedded in the phospholipid membrane in vivo, cytochrome c mediating electron transfer between amicyanin and the terminal oxidase must have some structural interaction with the terminal oxidase.

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