Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.12.7.2 (hydrogenase)
 3,522 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A biomimetic approach has been used to develop an artificial hydrogenase that catalyses the efficient reduction of protons producing hydrogen gas. Analogous to the unique biological metal clusters found in hydrogenase enzymes, the engineered active sites are small, well-defined Pt clusters deposited on the interior of a heat shock protein cage architecture with stoichiometries of 150 to 1000 Pt per protein cage. The proton reduction reaction is driven by visible light through a coupled reaction with Ru(bpy)3(2+) and methyl viologen as an electron-transfer mediator. Hydrogen production rates are comparable to those of hydrogenase on a per protein basis and exceed production rates of other reported Pt-based catalysts. These results demonstrate the utility of a biomimetic approach toward addressing the needs of hydrogen production.
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PMID:Biomimetic synthesis of a H2 catalyst using a protein cage architecture. 1627 73

The design of a biomimetic and fully base metal photocatalytic system for photocatalytic proton reduction in a homogeneous medium is described. A synthetic pyridylphosphole-appended [FeFe] hydrogenase mimic was encapsulated inside a supramolecular zinc porphyrin-based metal-organic cage structure Fe4 (Zn-L)6 . The binding is driven by the selective pyridine-zinc porphyrin interaction and results in the catalyst being bound strongly inside the hydrophobic cavity of the cage. Excitation of the capsule-forming porphyrin ligands with visible light while probing the IR spectrum confirmed that electron transfer takes place from the excited porphyrin cage to the catalyst residing inside the capsule. Light-driven proton reduction was achieved by irradiation of an acidic solution of the caged catalyst with visible light.
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PMID:Photocatalytic Hydrogen Evolution by a Synthetic [FeFe] Hydrogenase Mimic Encapsulated in a Porphyrin Cage. 3011 2

Hydrogen as a renewable fuel is viable when produced sustainably via proton reduction catalysis (PRC). Many homogeneous electrocatalysts perform PRC with high rates, but they all require a large overpotential to drive the reaction. Natural hydrogenase enzymes achieve reversible PRC with potentials close to the thermodynamic equilibrium through confinement of the active site in a well-defined protein pocket. Inspired by nature, we report a strategy that relies on the selective encapsulation of a synthetic hydrogenase mimic in a novel supramolecular cage. Catalyst confinement decreases the PRC overpotential by 150 mV, and is proposed to originate from the cationic cage stabilizing anionic reaction intermediates within the catalytic cycle.
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PMID:Control of the overpotential of a [FeFe] hydrogenase mimic by a synthetic second coordination sphere. 3078 63