A Soluble Cytochrome P-450 Functional in Methylene Hydroxylation

作者：Masato Katagiri, B. N. GANGULI, IRWIN C. GUNSALUS · 发表于：Journal of Biological Chemistry · 年份：1968 · DOI：10.1016/s0021-9258(18)93343-0 · 被引用次数：438 · 研究领域：Pharmacogenetics and Drug Metabolism、Porphyrin Metabolism and Disorders、Metabolism and Genetic Disorders

1. 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.