A site-differentiated [4Fe–4S] cluster controls electron transfer reactivity of <i>Clostridium acetobutylicum</i> [FeFe]-hydrogenase I
Carolyn E. Lubner, Jacob H. Artz, David W. Mulder, Aisha Oza, Rachel J. Ward, S. Garrett Williams, Anne K. Jones, John W. Peters, Ivan I. Smalyukh, Vivek S. Bharadwaj, Paul W. King
Abstract
Histidine coordination of the distal [4Fe–4S] cluster in [FeFe]-hydrogenase was demonstrated to tune the cluster spin-states, spin-pairing and surrounding molecular orbitals to enable more facile electron transfer compared to cysteine coordination.
Topics & Concepts
Clostridium acetobutylicumChemistryElectron transferRedoxHydrogenaseReactivity (psychology)FerredoxinElectron acceptorIntramolecular forcePhotochemistryMoleculeCatalysisStereochemistryEnzymeInorganic chemistryBiochemistryOrganic chemistryButanolPathologyEthanolMedicineAlternative medicineMetalloenzymes and iron-sulfur proteinsElectrocatalysts for Energy ConversionCO2 Reduction Techniques and Catalysts