The [FeFe]-hydrogenase maturation protein HydF contains a H-cluster like [4Fe4S]-2Fe site.
Formation of the catalytic six-iron complex (H-cluster) of [FeFe]-hydrogenase (HydA) requires its interaction with a specific maturation protein, HydF. Comparison by X-ray absorption spectroscopy at the Fe K-edge of HydF from Clostridium acetobutylicum and HydA1 from Chlamydomonas reinhardtii revealed that the overall structure of the iron site in both proteins is highly similar, comprising a [4Fe4S] cluster (Fe-Fe distances of ∼2.7Å) and a di-iron unit (Fe-Fe distance of ∼2.5Å). Thus, a precursor of the whole H-cluster is assembled on HydF. Formation of the core structures of both the 4Fe and 2Fe units may require only the housekeeping [FeS] cluster assembly machinery of the cell. Presumably, only the 2Fe cluster is transferred from HydF to HydA1, thereby forming the active site.
Ruhr-Universität Bochum, Lehrstuhl für Biochemie der Pflanzen, AG Photobiotechnologie, Bochum, Germany.
Ilka
I
Czech
Sven
S
Stripp
Oliver
O
Sanganas
Nils
N
Leidel
Thomas
T
Happe
Michael
M
Haumann
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D016825:Chlamydomonas reinhardtii / Q000201:enzymology*; D046969:Clostridium acetobutylicum / Q000201:enzymology*; D006859:Hydrogen / Q000737:chemistry / Q000378:metabolism; D006864:Hydrogenase / Q000737:chemistry / Q000378:metabolism*; D007501:Iron / Q000737:chemistry / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D056928:X-Ray Absorption Spectroscopy / Q000379:methods
D001426:Bacterial Proteins; D007506:Iron-Sulfur Proteins; D006859:Hydrogen; D007501:Iron; C118830:iron hydrogenase; D006864:Hydrogenase