A perspective on conformational control of electron transfer in nitric oxide synthases.
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.
Manchester Institute of Biotechnology, The University of Manchester, Manchester, United Kingdom.
Tobias M
TM
Hedison
Manchester Institute of Biotechnology, The University of Manchester, Manchester, United Kingdom.
Sam
S
Hay
Manchester Institute of Biotechnology, The University of Manchester, Manchester, United Kingdom. Electronic address: nigel.scrutton@manchester.ac.uk.
Nigel S
NS
Scrutton
D009251:NADPH-Ferrihemoprotein Reductase / Q000737:chemistry*; D019001:Nitric Oxide Synthase / Q000737:chemistry*; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence
D019001:Nitric Oxide Synthase; D009251:NADPH-Ferrihemoprotein Reductase
Cytochrome P450 reductase; Diflavin oxidoreductase; Fluorescence; Nitric oxide synthase; Protein dynamics