Abstract
A methylene hydroxylase system from camphor induced Pseudomonas putida has been separated into a putidaredoxin reductase, putidaredoxin (an iron-sulfur protein), and a hydroxylase fraction known as soluble cytochrome P-450 (1). This mixed function oxidase catalyzes the hydroxylation of methylene carbon 5 of camphor with reduced diphosphopyridine nucleotide as the primary electron donor and with molecular oxygen as the acceptor. The physicochemical and kinetic properties of the hydroxylase system are discussed in review articles by Gunsalus et al (2,3 and see articles by Gunsalus and Sligar in this book).
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© 1976 Plenum Press, New York
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Tanaka, M., Zeitlin, S., Yasunobu, K.T., Gunsalus, I.C. (1976). Current Status of the Sequence Studies of the Pseudomonas Putida Camphor Hydroxylase System. In: Yasunodu, K.T., Mower, H.F., Hayaishi, O. (eds) Iron and Copper Proteins. Advances in Experimental Medicine and Biology, vol 74. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3270-1_19
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DOI: https://doi.org/10.1007/978-1-4684-3270-1_19
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