Metalloenzymes and iron-sulfur proteins

Metalloenzymes built around iron-sulfur clusters carry out some of the most chemically demanding reactions in biology, including the reduction of protons to hydrogen gas and the fixation of atmospheric nitrogen into ammonia — processes that underpin the global cycles of energy and nutrients. Hydrogenases, a family of these enzymes, accomplish reversible hydrogen catalysis at rates and efficiencies that synthetic chemists have long struggled to match, making them central objects of study for anyone seeking to design better electrocatalysts for clean fuel production. A core challenge is understanding precisely how the geometry and electronic environment of iron-sulfur active sites enable such performance, which has driven a parallel effort to build biomimetic molecular models that replicate key structural features outside the protein scaffold. Integrating hydrogenases into artificial photosynthetic assemblies — so that sunlight can drive hydrogen production directly — remains an open and actively pursued direction, as does clarifying how cells assemble and repair these intricate metal clusters under physiological conditions.

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Keywords

HydrogenasesNitrogen FixationIron-Sulfur ClustersMolecular CatalysisElectrocatalytic Hydrogen ProductionBiomimetic Models