Metalloenzymes and iron-sulfur proteins

Metalloenzymes built around iron-sulfur clusters carry out some of biology's most chemically demanding reactions, including the splitting and production of molecular hydrogen by hydrogenases and the reduction of atmospheric nitrogen to ammonia by nitrogenase. Understanding how these proteins achieve such reactions under mild conditions — where synthetic industrial processes require extreme heat and pressure — has become a central problem for researchers trying to design cleaner energy technologies. Active work is focused on building biomimetic small molecules that replicate the geometry and reactivity of enzyme active sites well enough to drive electrocatalytic hydrogen production without precious metals. A parallel challenge is integrating natural or engineered hydrogenases into photosynthetic systems so that sunlight can power fuel generation directly, which requires reconciling the oxygen sensitivity of most hydrogenases with the oxygen-evolving environment of photosynthesis.

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Keywords

HydrogenasesNitrogen FixationIron-Sulfur ClustersMolecular CatalysisElectrocatalytic Hydrogen ProductionBiomimetic Models