Metabolism of Pipecolic Acid in a Pseudomonas Species IV. Electron Transport Particle of Pseudomonas putida

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Baginsky, Marietta L. (University of California, San Francisco Medical Center, San Francisco), and Victor W. Rodwell. Metabolism of pipecolic acid in a Pseudomonas species. IV. Electron transport particle of Pseudomonas putida. J. Bacteriol. 92:424–432. 1966.—Enzymes of Pseudomonas putida P2 catalyzing oxidation of pipecolate to Δ1-piperideine-6-carboxylate are located in a subcellular fraction sedimenting at 105,000 × g. Since this fraction resembles the mammalian electron transport particle in both chemical composition and enzymatic activities, it was termed Pseudomonas P2 electron transport particle (P2-ETP). P2-ETP contains flavin adenine dinucleotide, flavin mononucleotide, iron, copper, and both b- and c-type cytochromes. The reduced type b cytochrome has absorption maxima at 558 to 559, 530, and 427 mμ. Its oxidized pyridine hemochromogen has an absorption maximum at 406 mμ, with a shoulder at 564 mμ. On dithionite reduction, absorption bands with maxima at 556, 522, and 418 mμ are obtained. The reduced type c cytochrome has absorption maxima at 552, 520, and 422 mμ; its reduced pyridine hemochromogen has maxima at 551, 516 to 519, and 418 mμ. No type a cytochrome was detected. P2-ETP catalyzes oxidation of pipecolate and of reduced nicotinamide adenine dinucleotide (NADH2) by oxygen. It can also oxidize these compounds, as well as succinate and reduced nicotinamide adenine dinucleotide phosphate, with 2,6-dichlorophenol-indophenol as electron acceptor. Mammalian cytochrome c can be used as an alternate artificial electron acceptor for the oxidation of pipecolate and succinate, but not for oxidation of NADH2.

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