Artificial water-soluble systems inspired by [FeFe]-hydrogenases for electro- and photocatalytic hydrogen production
Sign Up to like & getrecommendations! Published in 2020 at "International Journal of Hydrogen Energy"
DOI: 10.1016/j.ijhydene.2019.11.206
Abstract: Abstract [FeFe]-hydrogenases efficiently catalyze the hydrogen evolution reactions (HERs) at rates of up to 104 sā1 with low overpotentials in aqueous media. Although the small-molecule diiron mimetics of the active site of [FeFe]-hydrogenases have been… read more here.
Keywords: fefe hydrogenases; systems inspired; water soluble; soluble systems ... See more keywords
Thermodynamic Hydricity of [FeFe]-Hydrogenases.
Sign Up to like & getrecommendations! Published in 2019 at "Journal of the American Chemical Society"
DOI: 10.1021/jacs.8b13084
Abstract: After remaining elusive for many years, terminal hydride states have now been identified in several native and mutant [FeFe]-hydrogenases. In this Perspective, hydride states of [FeFe]-hydrogenases are considered on the basis of hydricity, a thermodynamic… read more here.
Keywords: hydride; fefe hydrogenases; hydricity; thermodynamic hydricity ... See more keywords
Shedding light on proton and electron dynamics in [FeFe] hydrogenases.
Sign Up to like & getrecommendations! Published in 2020 at "Journal of the American Chemical Society"
DOI: 10.1021/jacs.9b13075
Abstract: [FeFe] hydrogenases are highly efficient catalysts for reversible dihydrogen evolution. H2 turnover involves different catalytic intermediates including a recently characterized hydride state of the active site (H-cluster). Applying cryogenic infrared and electron paramagnetic resonance spectroscopy… read more here.
Keywords: electron dynamics; fefe hydrogenases; electron; proton electron ... See more keywords
Accumulating the hydride state in the catalytic cycle of [FeFe]-hydrogenases
Sign Up to like & getrecommendations! Published in 2017 at "Nature Communications"
DOI: 10.1038/ncomms16115
Abstract: H2 turnover at the [FeFe]-hydrogenase cofactor (H-cluster) is assumed to follow a reversible heterolytic mechanism, first yielding a proton and a hydrido-species which again is double-oxidized to release another proton. Three of the four presumed… read more here.
Keywords: state; fefe hydrogenases; hydride state; state catalytic ... See more keywords
Air-stable [FeFe] hydrogenases
Sign Up to like & getrecommendations! Published in 2018 at "Nature Catalysis"
DOI: 10.1038/s41929-018-0137-y
Abstract: Hydrogenases are appealing catalysts for fuel cells, as these highly efficient H2-oxidation enzymes do not contain expensive precious metals and operate under very mild and safe conditions. Unfortunately, [FeFe] hydrogenases ā the most active class… read more here.
Keywords: fuel cells; coordination; fefe hydrogenases; air ... See more keywords
Binding of exogenous cyanide reveals new active-site states in [FeFe] hydrogenases
Sign Up to like & getrecommendations! Published in 2023 at "Chemical Science"
DOI: 10.1039/d2sc06098a
Abstract: [FeFe] hydrogenases are highly efficient metalloenyzmes for hydrogen conversion. Their active site cofactor (the H-cluster) is composed of a canonical [4Fe-4S] cluster ([4Fe-4S]H) linked to a unique organometallic di-iron subcluster ([2Fe]H). In [2Fe]H the two… read more here.
Keywords: new active; binding exogenous; site states; active site ... See more keywords
Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases.
Sign Up to like & getrecommendations! Published in 2018 at "Nature Communications"
DOI: 10.2210/pdb6gm1/pdb
Abstract: The unmatched catalytic turnover rates of [FeFe]-hydrogenases require an exceptionally efficient proton-transfer (PT) pathway to shuttle protons as substrates or products between bulk water and catalytic center. For clostridial [FeFe]-hydrogenase CpI such a pathway has… read more here.
Keywords: fefe hydrogenases; proton; proton transfer; transfer pathway ... See more keywords
Complex Multimeric [FeFe] Hydrogenases: Biochemistry, Physiology and New Opportunities for the Hydrogen Economy
Sign Up to like & getrecommendations! Published in 2018 at "Frontiers in Microbiology"
DOI: 10.3389/fmicb.2018.02911
Abstract: Hydrogenases are key enzymes of the energy metabolism of many microorganisms. Especially in anoxic habitats where molecular hydrogen (H2) is an important intermediate, these enzymes are used to expel excess reducing power by reducing protons… read more here.
Keywords: biochemistry; fefe hydrogenases; physiology; complex multimeric ... See more keywords
The Beta Subunit of Non-bifurcating NADH-Dependent [FeFe]-Hydrogenases Differs From Those of Multimeric Electron-Bifurcating [FeFe]-Hydrogenases
Sign Up to like & getrecommendations! Published in 2020 at "Frontiers in Microbiology"
DOI: 10.3389/fmicb.2020.01109
Abstract: A non-bifurcating NADH-dependent, dimeric [FeFe]-hydrogenase (HydAB) from Syntrophus aciditrophicus was heterologously produced in Escherichia coli, purified and characterized. Purified recombinant HydAB catalyzed NAD+ reduction coupled to hydrogen oxidation and produced hydrogen from NADH without the… read more here.
Keywords: non bifurcating; bifurcating nadh; hydrogen; fefe hydrogenases ... See more keywords
Fantastic [FeFe]-Hydrogenases and Where to Find Them
Sign Up to like & getrecommendations! Published in 2022 at "Frontiers in Microbiology"
DOI: 10.3389/fmicb.2022.853626
Abstract: [FeFe]-hydrogenases are complex metalloenzymes, key to microbial energy metabolism in numerous organisms. During anaerobic metabolism, they dissipate excess reducing equivalents by using protons from water as terminal electron acceptors, leading to hydrogen production. This reaction… read more here.
Keywords: fantastic fefe; fefe hydrogenases; hydrogenases find; physiology ... See more keywords