NO news is good news.
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.
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Department of Molecular Biology and Biochemistry, University of California, Irvine 92697-3900, USA. poulos@uci.edu
Raman
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D001665:Binding Sites; D002711:Chloride Peroxidase / Q000737:chemistry / Q000378:metabolism; D005486:Flavin Mononucleotide / Q000378:metabolism; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D008958:Models, Molecular; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D009251:NADPH-Ferrihemoprotein Reductase; D009569:Nitric Oxide / Q000378:metabolism; D019001:Nitric Oxide Synthase / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation
D005182:Flavin-Adenine Dinucleotide; D009569:Nitric Oxide; D005486:Flavin Mononucleotide; D002711:Chloride Peroxidase; D019001:Nitric Oxide Synthase; D009247:NADH, NADPH Oxidoreductases; D009251:NADPH-Ferrihemoprotein Reductase