4.4 Article

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

Journal

NITRIC OXIDE-BIOLOGY AND CHEMISTRY
Volume 63, Issue -, Pages 61-67

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.niox.2016.09.002

Keywords

Nitric oxide synthase; Cytochrome P450 reductase; Diflavin oxidoreductase; Fluorescence; Protein dynamics

Funding

  1. BBSRC/Bruker
  2. UK Biotechnology and Biological Sciences Research Council
  3. Engineering and Physical Sciences Research Council [EP/J020192/1]
  4. BBSRC [BB/H021523/1, BB/M017702/1] Funding Source: UKRI
  5. EPSRC [EP/J020192/1] Funding Source: UKRI
  6. Biotechnology and Biological Sciences Research Council [1225834, BB/H021523/1, BB/M017702/1] Funding Source: researchfish
  7. Engineering and Physical Sciences Research Council [EP/J020192/1] Funding Source: researchfish

Ask authors/readers for more resources

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 cyto chrome 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. (C) 2016 The Authors. Published by Elsevier Inc.

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