![]() Particularly, this reviews aims at giving an overview of the exquisite adaptability of heme, from bacteria to mammals. Please contact CBSC at cbscdgs.ca.gov if you have challenges accessing the codes. It describes at the molecular level the chemical capabilities of heme to achieve very different tasks and emphasizes how the properties of heme are determined by the protein structure. The active links below will take you to each publishers website. This review focusses on the mechanisms of allosteric protein activation triggered by heme coordination changes following diatomic binding to proteins as diverse as the human NO-receptor, cytochromes, NO-transporters and sensors, and a heme-activated potassium channel. ![]() Besides the properties of iron, proteins may impose a particular heme geometry leading to distortion, which allows selection or modulation of the electronic properties of heme. Their efficacy resides in the ability of heme to transmit both iron coordination changes and iron redox state changes to the protein structure. Allosteric heme proteins can fulfill a very large number of different functions thanks to the remarkable chemical versatility of heme through the entire living kingdom.
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