Recent advances in heme-protein sensors.
In recent years, an increasing number of proteins have been discovered which utilize heme cofactors to sense oxygen, carbon monoxide and nitric oxide. The identification and characterization of these proteins are revising our understanding of heme-mediated allostery first established in the early 1960s. Biochemical and structural studies are revealing new mechanisms for heme-driven conformational changes distinct from the classical hemoglobin model.
Departments of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210-1173, USA. chan@chemistry.ohio-state.edu
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D000494:Allosteric Regulation / Q000502:physiology; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D015374:Biosensing Techniques; D002248:Carbon Monoxide / Q000378:metabolism; D006418:Heme / Q000737:chemistry / Q000378:metabolism*; D006420:Hemeproteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry / Q000378:metabolism; D009569:Nitric Oxide / Q000378:metabolism; D010100:Oxygen / Q000378:metabolism; D011487:Protein Conformation
D001426:Bacterial Proteins; D006420:Hemeproteins; D009211:Myoglobin; D009569:Nitric Oxide; D006418:Heme; D002248:Carbon Monoxide; D010100:Oxygen