Studies on FAD- and FMN-binding domains in NADPH-cytochrome P-450 reductase from rabbit liver microsomes.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference39 articles.
1. Redox properties of the reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 and reduced nicotinamide adenine dinucleotide-cytochrome b5 reductases
2. Studies on the microsomal mixed function oxidase system: redox properties of detergent-solubilized NADPH-cytochrome P-450 reductase
3. NADPH-cytochrome c (P-450) reductase. Spectrophotometric and stopped flow kinetic studies on the formation of reduced flavoprotein intermediates.
4. Identification of the high and low potential flavins of liver microsomal NADPH-cytochrome P-450 reductase.
5. Separate roles for FMN and FAD in catalysis by liver microsomal NADPH-cytochrome P-450 reductase.
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