Edna Stewart Rose Hills
Biochemical Characterization of a CO-Activated Soluble Guanylate Cyclase (sGC)
In mammals, soluble guanylate cyclase (sGC) serves as the primary receptor for the signaling gas nitric oxide (NO). Binding of NO activates the enzyme, which leads to various signaling pathways that regulate many physiological functions, including vasodilation and neurotransmission. Activators of sGC are currently used as therapeutic agents for cardiopulmonary and urogenital diseases. I will be investigating an sGC homolog called Cyg11 present in the alga Chlamydomonas reinhardtii. Preliminary results indicate that carbon monoxide activates the algal homolog more compared to nitric oxide, a novel activity that warrants complete biochemical characterization. Thus, I plan to obtain a complete enzymatic activity profile with different ligands bound to Cyg11. Investigating this novel CO activation in C. reinhardtii sGC may provide insights that add to our understanding of NO stimulation of mammalian sGC.