The [FeFe]-hydrogenase maturase HydF from Clostridium acetobutylicum contains a CO and CN ligated iron cofactor |
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Authors: | Ilka Czech Alexey Silakov Wolfgang Lubitz |
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Affiliation: | a Lehrstuhl Biochemie der Pflanzen, AG Photobiotechnologie, Ruhr Universität Bochum, Universitätsstrasse 150, 44801 Bochum, Germany b Max-Planck-Institut für Bioanorganische Chemie, 45470 Mülheim an der Ruhr, Germany |
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Abstract: | Biosynthesis of the [FeFe] hydrogenases active site (H-cluster) requires three maturation factors whose respective roles are not understood yet. The clostridial maturation enzymes (CaHydE, CaHydF and CaHydG) were homologously overexpressed in their native host Clostridium acetobutylicum. CaHydF was able to activate Chlamydomonas reinhardtii [FeFe] hydrogenase apoprotein (CrHydA1apo) to almost 100% compared to the native specific hydrogen evolution activity. Based on electron paramagnetic resonance spectroscopy and Fourier-transform infrared spectroscopy data the existence of a [4Fe4S] cluster and a CO and CN− ligand coordinated di-iron cluster is suggested. This study contains the first experimental evidence that the bi-nuclear part of the H-cluster is assembled in HydF. |
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Keywords: | EPR, electron paramagnetic resonance spectroscopy FTIR, Fourier-transform infrared spectroscopy HYSCORE, Hyperfine sublevel correlation spectroscopy CrHydA1, [FeFe] hydrogenase protein of C. reinhardtii CaHydE, maturation factor HydE of C. acetobutylicum CaHydF, maturation factor HydF of C. acetobutylicum CaHydG, maturation factor HydG of C. acetobutylicum TmHydE, maturation factor HydE of Thermotoga maritima TmHydF, maturation factor HydF of Thermotoga maritima [2Fe]H, [2Fe2S] moiety of the H-cluster GTP, Guanosintriphosphate GDP, Guanosindiphosphate SAM, S-adenosyl methionine AdoH, 5&prime -Desoxyadenosine |
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