Iron and Copper Proteins pp 263-269 | Cite as
Current Status of the Sequence Studies of the Pseudomonas Putida Camphor Hydroxylase System
Chapter
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).
Keywords
Hydroxylase System Putidaredoxin Reductase Bovine Adrenodoxin Reduce Diphosphopyridine Nucleotide
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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© Plenum Press, New York 1976