The [4Fe-4S] Cluster of HydF Is Essential for [FeFe]-Hydrogenase Maturation.

ABSTRACT: The organometallic H-cluster of the [FeFe]-hydrogenase is assembled in vivo through a complex process requiring the action of three dedicated maturation enzymes, HydG, HydE, and HydF, as well as the aminomethyl-lipoyl-H-protein (H_met) of the glycine cleavage system (GCS). Here we probe the role of HydF and its [4Fe-4S] cluster in [FeFe]-hydrogenase maturation by using a defined semisynthetic approach in which [Fe^I₂(μ-SH)₂(CO)₄(CN)₂]^2- ([2Fe]_E) is used to bypass HydE and HydG, and GCS components are used in place of cell lysate. We show that inclusion of the iron-sulfur carrier protein NfuA and the high-CO-affinity myoglobin variant Mb^H64L provides dramatically improved hydrogenase acti

SUBMITTER: Balci B 

PROVIDER: S-EPMC12752695 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature