Molecular aspects of sGC regulation
© Marletta et al; licensee BioMed Central Ltd. 2011
Published: 1 August 2011
Ferric heme oxidized sGC has low activity, and the NO complex of the re-reduced heme generates a desensitized, low-activity state of sGC. The molecular mechanism for this desensitization involves site specific S-nitrosation. The conformational changes associated with activation are both subtle and complex. Hydrogen-deuterium exchange mass spectrometry analysis can be used to probe conformational changes and protein-protein interactions. This method has been brought to bear on sGC, illuminating domain interactions within sGC and conformational changes induced by NO binding.
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