Metalloenzymes and iron-sulfur proteins

Metalloenzymes built around iron-sulfur clusters carry out some of biology's most energetically demanding reactions, including the splitting and production of molecular hydrogen by hydrogenases and the reduction of atmospheric nitrogen to ammonia. Understanding how these proteins achieve such chemistry with earth-abundant metals, at mild temperatures and pressures, has direct implications for designing synthetic catalysts that could underpin a cleaner energy economy. Researchers are currently working to decode precise structure-function relationships within enzyme active sites and to translate those principles into biomimetic molecular catalysts capable of electrocatalytic hydrogen production. Open questions remain around how iron-sulfur clusters are assembled and protected inside living cells, and how hydrogenases might be stably integrated into artificial photosynthetic systems to drive fuel production from sunlight.

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Keywords

HydrogenasesNitrogen FixationIron-Sulfur ClustersMolecular CatalysisElectrocatalytic Hydrogen ProductionBiomimetic Models