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)

The unique photochemical properties of Ru(II)-diimine complexes have helped initiate a series of seminal electron transfer studies in metalloenzymes. It has thus been possible to experimentally determine rate constants for long-range electron transfers. These studies have laid the foundation for the investigation of reactive intermediates in heme proteins and for the design of light-activated biocatalysts. Various metalloenzymes such as hydrogenase, carbon monoxide dehydrogenase, nitrogenase, laccase and cytochrome P450 BM3 have been functionalized with Ru(II)-diimine complexes. Upon visible light-excitation, these photosensitized metalloproteins are capable of sustaining photocatalytic activity to reduce small molecules such as protons, acetylene, hydrogen cyanide and carbon monoxide or activate molecular dioxygen to produce hydroxylated products. The Ru(II)-diimine photosensitizers are hence able to deliver multiple electrons to metalloenzymes buried active sites, circumventing the need for the natural redox partners. In this review, we will highlight the key achievements of the light-driven biocatalysts, which stem from the extensive electron transfer investigations. This article is part of a Special Issue entitled Biodesign for Bioenergetics--the design and engineering of electronic transfer cofactors, proteins and protein networks, edited by Ronald L. Koder and J.L. Ross Anderson.
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PMID:Ru(II)-diimine functionalized metalloproteins: From electron transfer studies to light-driven biocatalysis. 2639 47

In this review, we have portrayed the structure, synthesis and applications of a variety of biomimetic MOFs from an unprecedented angle. Synthetic MOF analogues of five distinct enzymes: phosphotriesterase, hydrogenase, cytochrome P450, chymotrypsin and carbonic anhydrase, have been discussed with their skeletal comparison to actual enzymatic active sites as reference, and an explanation of catalytic pathways from the mechanistic cycle of the corresponding enzymes is depicted. We demonstrated critically each of the five discrete situations by assimilating available benchmark researches in an attempt to provide a concise literature source on the ingenious design strategies and versatile biomimetic applications of this domain of materials.
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PMID:Metal organic frameworks mimicking natural enzymes: a structural and functional analogy. 2725 Nov 15

Visible light-driven redox reactions have been widely adopted for the production of chemicals to combat energy shortage and global warming. Key elements of such a reaction system include a photosensitizer, a catalyst, and an electron source. In this review, we introduce the small molecules and nanoparticles that are widely used as photosensitizers, as well as the development of a photosensitizer protein that is based on the expansion of genetic code, with a fluorescent protein that is used as a scaffold. Visible light-driven enzymes using proteins as photosensitizers or as catalysts such as carbon monoxide dehydrogenase (CODH), formic acid dehydrogenase (FDH), hydrogenase, nitrogenase, cytochrome P450 BM3, and alkane synthase are then described. CODH can be coupled with photosensitizing nanoparticles to reduce CO2 to CO, and hydrogenase can produce H2 using high-energy electrons produced from dye-sensitized nanoparticles. When water-soluble zinc porphyrin is coupled with FDH, visible light drives CO2 to produce formic acid. Nitrogenase can reduce N2 to NH3 using CdS nanoparticle as photosensitizer. Cytochrome P450 BM3 can be enhanced by a visible light-driven redox system and thus by hydroxylate lauric acid or fatty acids. CvFAP, an alkane synthase, can decarboxylate palmitic acid to pentadecane under blue light excitation. Moreover, we describe a genetically encoded photosensitive protein, which mimics the function of natural photosynthesis and catalyzes the conversion of CO2 to CO when covalently attached with a Ni-terpyridine complex.
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PMID:Coupling natural systems with synthetic chemistry for light-driven enzymatic biocatalysis. 3131 82