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Methods in Molecular Biology, ISSN 1064-3745, 2019, Volume 1876, pp. 65 - 88
Journal Article
FEBS Letters, ISSN 0014-5793, 2010, Volume 584, Issue 3, pp. 638 - 642
Biosynthesis of the [FeFe] hydrogenases active site (H-cluster) requires three maturation factors whose respective roles are not understood yet... 
Clostridium acetobutylicum | H-Cluster | Fourier-transform infrared spectroscopy | Maturation | [FeFe] Hydrogenase | Electron paramagnetic resonance spectroscopy | GTP | EPR | [2Fe]H | [FeFe] hydrogenase protein of C. reinhardtii | CrHydA1 | Guanosindiphosphate | HYSCORE | Guanosintriphosphate | TmHydE | GDP | TmHydF | FTIR | maturation factor HydG of C. acetobutylicum | 5′-Desoxyadenosine | maturation factor HydE of C. acetobutylicum | CaHydG | maturation factor HydE of Thermotoga maritima | CaHydE | CaHydF | AdoH | Hyperfine sublevel correlation spectroscopy | [2Fe2S] moiety of the H-cluster | maturation factor HydF of C. acetobutylicum | maturation factor HydF of Thermotoga maritima | S-adenosyl methionine | electron paramagnetic resonance spectroscopy | SAM | ACTIVATION | ACTIVE-SITE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SULFUR PROTEINS | FEFE HYDROGENASE | CELL BIOLOGY | BIOPHYSICS | SPECTROSCOPY | BIOSYNTHESIS | ENZYMES | ALGA CHLAMYDOMONAS-REINHARDTII | THERMOTOGA-MARITIMA | Clostridium acetobutylicum - genetics | Hydrogenase - genetics | Electrophoresis, Polyacrylamide Gel | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Iron-Sulfur Proteins - genetics | Carbon Monoxide - chemistry | Hydrogenase - chemistry | Iron-Sulfur Proteins - chemistry | Spectroscopy, Fourier Transform Infrared | Hydrogenase - metabolism | Bacterial Proteins - metabolism | Iron-Sulfur Proteins - metabolism | Clostridium acetobutylicum - enzymology | Hydrogen - metabolism
Journal Article
Journal Article
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 03/2017, Volume 139, Issue 12, pp. 4306 - 4309
[FeFe]-hydrogenases catalyze the reversible reduction of protons to molecular hydrogen with extremely high efficiency. The active site (“H-cluster”) consists of a [4Fe–4S... 
FEFE HYDROGENASES | ACTIVATION | MODELS | ACTIVE-SITE | LIGAND | IDENTIFICATION | CHEMISTRY, MULTIDISCIPLINARY | HYDROGENASE H-CLUSTER | CATALYTIC CYCLE | Chemical bonds | Nuclear magnetic resonance spectroscopy | Usage | Iron compounds | Chemical properties | Analysis
Journal Article
Catalysis today, ISSN 0920-5861, 2018, Volume 316, pp. 223 - 229
A novel [FeFe]-hydrogenase biomimetic catalyst [(μ-dmedt)Fe2(CO)5](μ-DPPF-O) (1) was prepared and used as catalyst for phenol hydroxylation with excellent dihydroxybenzene selectivity (94.0... 
Phenol | DPPF | [FeFe]-Hydrogenase | Hydroxylation | Dihydroxybenzene | BENZENE | ACTIVE-SITE | DIIRON COMPLEXES | PERFORMANCE | CHEMISTRY, PHYSICAL | H2O2 | OXIDE CATALYSTS | ENGINEERING, CHEMICAL | PENTACOORDINATE IRON DICARBONYL | NITROGEN HETEROCYCLIC CARBENE | PROTON REDUCTION | CHEMISTRY, APPLIED | HYDROGENASE
Journal Article