A Conserved Binding Pocket in HydF is Essential for Biological Assembly and Coordination of the Diiron Site of [FeFe]-Hydrogenases.
In: Journal of the American Chemical Society, Jg. 146 (2024-06-12), Heft 23, S. 15771-15778
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Zugriff:
The active site cofactor of [FeFe]-hydrogenases consists of a cubane [4Fe-4S]-cluster and a unique [2Fe-2S]-cluster, harboring unusual CO- and CN - -ligands. The biosynthesis of the [2Fe-2S]-cluster requires three dedicated maturation enzymes called HydG, HydE and HydF. HydG and HydE are both involved in synthesizing a [2Fe-2S]-precursor, still lacking parts of the azadithiolate (adt) moiety that bridge the two iron atoms. This [2Fe-2S]-precursor is then finalized within the scaffold protein HydF, which binds and transfers the [2Fe-2S]-precursor to the hydrogenase. However, its exact binding mode within HydF is still elusive. Herein, we identified the binding location of the [2Fe-2S]-precursor by altering size and charge of a highly conserved protein pocket via site directed mutagenesis (SDM). Moreover, we identified two serine residues that are essential for binding and assembling the [2Fe-2S]-precursor. By combining SDM and molecular docking simulations, we provide a new model on how the [2Fe-2S]-cluster is bound to HydF and demonstrate the important role of one highly conserved aspartate residue, presumably during the bioassembly of the adt moiety.
Titel: |
A Conserved Binding Pocket in HydF is Essential for Biological Assembly and Coordination of the Diiron Site of [FeFe]-Hydrogenases.
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Autor/in / Beteiligte Person: | Haas, R ; Lampret, O ; Yadav, S ; Apfel, UP ; Happe, T |
Zeitschrift: | Journal of the American Chemical Society, Jg. 146 (2024-06-12), Heft 23, S. 15771-15778 |
Veröffentlichung: | Washington, DC : American Chemical Society ; <i>Original Publication</i>: Easton, Pa. [etc.], 2024 |
Medientyp: | academicJournal |
ISSN: | 1520-5126 (electronic) |
DOI: | 10.1021/jacs.4c01635 |
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