Iron–Sulfur Cluster States of the Hydrogenase Maturase HydF

Shepard, Eric M.; Byer, Amanda S.; Broderick, Joan B.

doi:10.1021/acs.biochem.7b00735

Cited by 6 publications

(1 citation statement)

References 5 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition to the [4Fe-4S] cluster, there is evidence from EPR spectroscopy that as-isolated and chemically reconstituted HydF can also host a [2Fe-2S] cluster [ 61 , 62 , 63 , 64 , 65 ], which is otherwise lacking in all solved HydF crystal structures [ 48 , 56 ]. Given this discrepancy, it is still unclear whether the presence of a [2Fe-2S] cluster represents a physiological state, a state of partial cluster maturation, or simply arises from an incomplete reconstitution due to the in vitro conditions.…”

Section: The Maturasesmentioning

confidence: 99%

Overview of the Maturation Machinery of the H-Cluster of [FeFe]-Hydrogenases with a Focus on HydF

Bortolus

Costantini

Doni

et al. 2018

IJMS

View full text Add to dashboard Cite

Hydrogen production in nature is performed by hydrogenases. Among them, [FeFe]-hydrogenases have a peculiar active site, named H-cluster, that is made of two parts, synthesized in different pathways. The cubane sub-cluster requires the normal iron-sulfur cluster maturation machinery. The [2Fe] sub-cluster instead requires a dedicated set of maturase proteins, HydE, HydF, and HydG that work to assemble the cluster and deliver it to the apo-hydrogenase. In particular, the delivery is performed by HydF. In this review, we will perform an overview of the latest knowledge on the maturation machinery of the H-cluster, focusing in particular on HydF.

show abstract