The [FeFe]-hydrogenase maturase HydF from Clostridium acetobutylicum contains a CO and CN- ligated iron cofactor

Ilka Czech; Alexey Silakov; Wolfgang Lubitz; Thomas Happe

doi:10.1016/j.febslet.2009.12.016

The [FeFe]-hydrogenase maturase HydF from Clostridium acetobutylicum contains a CO and CN^- ligated iron cofactor

Ilka Czech, Alexey Silakov, Wolfgang Lubitz, Thomas Happe

Chemistry

Research output: Contribution to journal › Article › peer-review

92 Scopus citations

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 (CrHydA1_apo) 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.

Original language	English (US)
Pages (from-to)	638-642
Number of pages	5
Journal	FEBS Letters
Volume	584
Issue number	3
DOIs	https://doi.org/10.1016/j.febslet.2009.12.016
State	Published - Feb 5 2010

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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title = "The [FeFe]-hydrogenase maturase HydF from Clostridium acetobutylicum contains a CO and CN- ligated iron cofactor",

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.",

author = "Ilka Czech and Alexey Silakov and Wolfgang Lubitz and Thomas Happe",

note = "Funding Information: This work was supported by the European Union/Energy Network ( SOLAR-H2 contract 212508), the BMBF (H 2 -design cells) and the Max-Planck-Gesellschaft. We are also very grateful to L. Currell (MPI M{\"u}lheim/Ruhr) for his technical assistance.",

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doi = "10.1016/j.febslet.2009.12.016",

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AU - Czech, Ilka

AU - Silakov, Alexey

AU - Lubitz, Wolfgang

AU - Happe, Thomas

N1 - Funding Information: This work was supported by the European Union/Energy Network ( SOLAR-H2 contract 212508), the BMBF (H 2 -design cells) and the Max-Planck-Gesellschaft. We are also very grateful to L. Currell (MPI Mülheim/Ruhr) for his technical assistance.

PY - 2010/2/5

Y1 - 2010/2/5

N2 - 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.

AB - 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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The [FeFe]-hydrogenase maturase HydF from Clostridium acetobutylicum contains a CO and CN^- ligated iron cofactor

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