Energy landscapes and catalysis in nitric-oxide synthase

Anna Sobolewska-Stawiarz, Nicole G H Leferink, Karl Fisher, Derren J. Heyes, Sam Hay, Stephen E J Rigby, Nigel S. Scrutton

Research output: Contribution to journalArticlepeer-review


Background: Protein domain dynamics and calmodulin binding are implicated in regulating electron flow in NO synthase. Results: A dynamic conformational landscape important for enzyme catalysis is demonstrated. Conclusion:NOsynthesis requires a complex landscape of conformations, with calmodulin as a key driver of chemistry through modulation of the dynamic landscape. Significance: Detailed understanding of conformational landscapes provides new opportunities for inhibitor discovery targeted at the dynamic interfaces. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
Original languageEnglish
Pages (from-to)11725-11738
Number of pages13
JournalJournal of Biological Chemistry
Issue number17
Publication statusPublished - 25 Apr 2014


  • Calmodulin
  • Enzyme Kinetics
  • Flavoproteins
  • Free Energy Landscapes
  • High Pressure Stopped Flow
  • Nitric-oxide Synthase
  • PELDOR Spectroscopy
  • Protein Dynamics


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