Electronic isomerism in a heterometallic nickel–iron–sulfur cluster models substrate binding and cyanide inhibition of carbon monoxide dehydrogenase
Luke C. Lewis, José A. Sanabria-Gracia, Yuri Lee, Adam J. Jenkins, Hannah S. Shafaat
Abstract
inhibits the native system while the CO-bound state continues to elude isolation in CODH. The detailed characterization of isolable states that are accessible in our CODH model system provides valuable insight into unresolved enzymatic intermediates and offers design principles towards developing functional mimics of CODH.
Topics & Concepts
CyanideCarbon monoxide dehydrogenaseCarbon monoxideNickelSulfurChemistrySubstrate (aquarium)Cluster (spacecraft)Inorganic chemistryPhotochemistryOrganic chemistryBiologyCatalysisComputer scienceProgramming languageEcologyMetalloenzymes and iron-sulfur proteinsMetal-Catalyzed Oxygenation MechanismsPorphyrin Metabolism and Disorders