Energy landscapes and catalysis in nitric-oxide synthase

Abstract

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.