Abstract
The recent determination of the crystal structure of microsomal cytochrome P450 reductase, a diflavin protein that shuttles electrons from NADPH to the P450 heme, represents a significant advance towards the understanding of cytochromes P450. A similar advance was made in a related enzyme system, nitric oxide synthase (NOS). The crystal structure of the NOS heme domain reveals a very different architecture to that observed in P450s and offers significant insight into the production of nitric oxide, one of nature's most important regulatory molecules.
Publication types
-
Research Support, Non-U.S. Gov't
-
Review
MeSH terms
-
Binding Sites
-
Chloride Peroxidase / chemistry
-
Chloride Peroxidase / metabolism
-
Flavin Mononucleotide / metabolism
-
Flavin-Adenine Dinucleotide / metabolism
-
Models, Molecular
-
NADH, NADPH Oxidoreductases / chemistry*
-
NADH, NADPH Oxidoreductases / metabolism
-
NADPH-Ferrihemoprotein Reductase
-
Nitric Oxide / metabolism
-
Nitric Oxide Synthase / chemistry*
-
Nitric Oxide Synthase / metabolism*
-
Protein Conformation
Substances
-
Flavin-Adenine Dinucleotide
-
Nitric Oxide
-
Flavin Mononucleotide
-
Chloride Peroxidase
-
Nitric Oxide Synthase
-
NADH, NADPH Oxidoreductases
-
NADPH-Ferrihemoprotein Reductase