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[FeFe]-hydrogenase ...
[FeFe]-hydrogenase maturation : H-cluster assembly intermediates tracked by electron paramagnetic resonance, infrared, and X-ray absorption spectroscopy
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- Németh, Brigitta (författare)
- Uppsala universitet,Molekylär biomimetik,Montana State Univ, Dept Chem & Biochem, Bozeman, MT 59717 USA.
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- Senger, Moritz (författare)
- Uppsala universitet,Fysikalisk kemi,Free Univ Berlin, Phys Dept, Mol Biophys, D-14195 Berlin, Germany.
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- Redman, Holly J. (författare)
- Uppsala universitet,Molekylär biomimetik
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- Ceccaldi, Pierre (författare)
- Uppsala universitet,Molekylär biomimetik
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- Broderick, Joan (författare)
- Montana State Univ, Dept Chem & Biochem, Bozeman, MT 59717 USA.
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- Magnuson, Ann (författare)
- Uppsala universitet,Molekylär biomimetik
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- Stripp, Sven T. (författare)
- Free Univ Berlin, Phys Dept, Mol Biophys, D-14195 Berlin, Germany.
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- Haumann, Michael (författare)
- Free Univ Berlin, Phys Dept, Biophys Metalloenzymes, D-14195 Berlin, Germany.
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- Berggren, Gustav (författare)
- Uppsala universitet,Molekylär biomimetik
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(creator_code:org_t)
- 2020-07-13
- 2020
- Engelska.
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Ingår i: Journal of Biological Inorganic Chemistry. - : Springer Nature. - 0949-8257 .- 1432-1327. ; 25:5, s. 777-788
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Abstract
Ämnesord
Stäng
- [FeFe]-hydrogenase enzymes employ a unique organometallic cofactor for efficient and reversible hydrogen conversion. This so-called H-cluster consists of a [4Fe-4S] cubane cysteine linked to a diiron complex coordinated by carbon monoxide and cyanide ligands and an azadithiolate ligand (adt =NH(CH2S)(2)).[FeFe]-hydrogenase apo-protein binding only the [4Fe-4S] sub-complex can be fully activated in vitro by the addition of a synthetic diiron site precursor complex ([2Fe](adt)). Elucidation of the mechanism of cofactor assembly will aid in the design of improved hydrogen processing synthetic catalysts. We combined electron paramagnetic resonance, Fourier-transform infrared, and X-ray absorption spectroscopy to characterize intermediates of H-cluster assembly as initiated by mixing of the apo-protein (HydA1) from the green alga Chlamydomonas reinhardtii with [2Fe](adt). The three methods consistently show rapid formation of a complete H-cluster in the oxidized, CO-inhibited state (Hox-CO) already within seconds after the mixing. Moreover, FTIR spectroscopy support a model in which Hox-CO formation is preceded by a short-lived Hred'-CO-like intermediate. Accumulation of Hox-CO was followed by CO release resulting in the slower conversion to the catalytically active state (Hox) as well as formation of reduced states of the H-cluster. [GRAPHICS] .
Ämnesord
- NATURVETENSKAP -- Kemi -- Teoretisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Theoretical Chemistry (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- Metalloenzymes
- [FeFe]-hydrogenase
- H-cluster assembly
- Time-resolved spectroscopy
- Maturation intermediates
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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