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June 1, 1968Journal of Biological Chemistry439 citationsOpen Access

A Soluble Cytochrome P-450 Functional in Methylene Hydroxylation

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MKMasato KatagiriBGB. N. GANGULIIGI. C. Gunsalus

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Abstract

A methylene hydroxylase system from camphor induced Pseudomonas putida strain C1 cells has been separated into three fractions: a putidaredoxin reductase, putidaredoxin (an iron-sulfur protein), and a hydroxylase (shown to be a soluble cytochrome P-450). 2. This system of enzymes catalyzes the hydroxylation of methylene carbon 5 of camphor with reduced disphosphopyridine nucleotide as a primary electron donor and molecular oxygen as acceptor. 3. The redoxin serves as the electron carrier from the reduced pyridine nucleotide and reductase to the cytochrome P-450-substrate complex. 4. The coupling of the hydroxylase (P-450) to the reduced diphosphopyridine nucleotide dehydrogenase (reductase), and the putidaredoxin is demonstrated, and substrate is shown to be required for the over-all reaction.

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Katagiri et al. (1968) studied this question.

synapsesocial.com/papers/6a20a7be6236d09b9bcd40b9https://doi.org/10.1016/s0021-9258(18)93343-0
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