Hydrogenases catalyze the formation of hydrogen. The cofactor ('H-cluster') of [FeFe]-hydrogenases consists of a [4Fe-4S] cluster bridged to a unique [2Fe] subcluster whose biosynthesis in vivo requires hydrogenase-specific maturases. Here we show that a chemical mimic of the [2Fe] subcluster can reconstitute apo-hydrogenase to full activity, independent of helper proteins. The assembled H-cluster is virtually indistinguishable from the native cofactor. This procedure will be a powerful tool for developing new artificial H₂-producing catalysts.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3795299PMC
http://dx.doi.org/10.1038/nchembio.1311DOI Listing

Publication Analysis

Top Keywords

[2fe] subcluster
8
spontaneous activation
4
activation [fefe]-hydrogenases
4
[fefe]-hydrogenases inorganic
4
inorganic [2fe]
4
[2fe] active
4
active site
4
site mimic
4
mimic hydrogenases
4
hydrogenases catalyze
4

Similar Publications

[FeFe]-hydrogenases efficiently catalyze the reversible oxidation of molecular hydrogen. Their prowess stems from the intricate H-cluster, combining a [Fe S ] center with a binuclear iron center ([2Fe] ). In the latter, each iron atom is coordinated by a CO and CN ligand, connected by a CO and an azadithiolate ligand.

View Article and Find Full Text PDF

[FeFe]-hydrogenases employ a catalytic H-cluster, consisting of a [4Fe-4S] cluster linked to a [2Fe] subcluster with CO, CN ligands, and an azadithiolate bridge, which mediates the rapid redox interconversion of H and H. In the biosynthesis of this H-cluster active site, the radical -adenosyl-l-methionine (radical SAM, RS) enzyme HydG plays the crucial role of generating an organometallic [Fe(II)(CN)(CO)(cysteinate)] product that is en route to forming the H-cluster. Here, we report direct observation of this diamagnetic organometallic Fe(II) complex through Mössbauer spectroscopy, revealing an isomer shift of δ = 0.

View Article and Find Full Text PDF

A Dynamic Water Channel Affects O Stability in [FeFe]-Hydrogenases.

ChemSusChem

February 2024

Faculty of Biology and Biotechnology, Photobiotechnology, Ruhr University Bochum, Universitätsstrasse 150, 44801, Bochum, Germany.

[FeFe]-hydrogenases are capable of reducing protons at a high rate. However, molecular oxygen (O ) induces the degradation of their catalytic cofactor, the H-cluster, which consists of a cubane [4Fe4S] subcluster (4Fe ) and a unique diiron moiety (2Fe ). Previous attempts to prevent O -induced damage have focused on enhancing the protein's sieving effect for O by blocking the hydrophobic gas channels that connect the protein surface and the 2Fe .

View Article and Find Full Text PDF

Evidence of Atypical Structural Flexibility of the Active Site Surrounding of an [FeFe] Hydrogenase from .

J Am Chem Soc

May 2023

Pennsylvania State University, 104 Chemistry Building, University Park, Pennsylvania 16802, United States.

[FeFe] hydrogenase from (HydA1) is an unusual hydrogenase in that it can withstand prolonged exposure to O by reversibly converting into an O-protected, inactive state (H). It has been indicated in the past that an atypical conformation of the "SCCP" loop near the [2Fe] portion of the six-iron active site (H-cluster) allows the Cys367 residue to adopt an "off-H-pathway" orientation, promoting a facile transition of the cofactor to H. Here, we investigated the electronic structure of the H-cluster in the oxidized state (H) that directly converts to H under oxidizing conditions and the related CO-inhibited state (H-CO).

View Article and Find Full Text PDF

[FeFe] hydrogenases are exceptionally active catalysts for the interconversion of molecular hydrogen with protons and electrons. Their active site, the H-cluster, is composed of a [4Fe-4S] cluster covalently linked to a unique [2Fe] subcluster. These enzymes have been extensively studied to understand how the protein environment tunes the properties of the Fe ions for efficient catalysis.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!