A perspective on conformational control of electron transfer in nitric oxide synthases

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Hedison, Tobias M. ; Hay, Sam ; Scrutton, Nigel S. (2017)
  • Publisher: Elsevier
  • Journal: Nitric Oxide, volume 63, pages 61-67 (issn: 1089-8603, eissn: 1089-8611)
  • Related identifiers: pmc: PMC5295631, doi: 10.1016/j.niox.2016.09.002
  • Subject: NOS, nitric oxide synthase | Protein dynamics | Physiology | FMN, flavin mononucleotide | MSR, methionine synthase reductase | FRET, Förster resonance energy transfer | Cytochrome P450 reductase | Cancer Research | Article | CPR, cytochrome P450 reductase | P450 BM3, cytochrome P450 BM3 | Fluorescence | FAD, flavin adenosine dinucleotide | Biochemistry | Clinical Biochemistry | Nitric oxide synthase | Diflavin oxidoreductase | CaM, calmodulin

This perspective reviews single molecule and ensemble fluorescence spectroscopy studies of the three tissue specific nitric oxide synthase (NOS) isoenzymes and the related diflavin oxidoreductase cytochrome P450 reductase. The focus is on the role of protein dynamics and the protein conformational landscape and we discuss how recent fluorescence-based studies have helped in illustrating how the nature of the NOS conformational landscape relates to enzyme turnover and catalysis.