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Monitoring H-cluster assembly using a semi-synthetic HydF protein

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Abstract

The [FeFe] hydrogenase enzyme interconverts protons and molecular hydrogen with remarkable efficiency. The reaction is catalysed by a unique metallo-cofactor denoted as the H-cluster containing an organometallic dinuclear Fe component, the [2Fe] subsite. The HydF protein delivers a precursor of the [2Fe] subsite to the apo-[FeFe] hydrogenase, thus completing the H-cluster and activating the enzyme. Herein we generate a semi-synthetic form of HydF by loading it with a synthetic low valent dinuclear Fe complex. We show that this semi-synthetic protein is practically indistinguishable from the native protein, and utilize this form of HydF to explore the mechanism of H-cluster assembly. More specifically, we show that transfer of the precatalyst from HydF to the hydrogenase enzyme results in the release of CO, underscoring that the pre-catalyst is a four CO species when bound to HydF. Moreover, we propose that an electron transfer reaction occurs during H-cluster assembly, resulting in an oxidation of the [2Fe] subsite with concomitant reduction of the [4Fe4S] cluster present on the HydF protein.

Graphical abstract: Monitoring H-cluster assembly using a semi-synthetic HydF protein

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Publication details

The article was received on 26 Oct 2018, accepted on 21 Dec 2018 and first published on 03 Jan 2019


Article type: Paper
DOI: 10.1039/C8DT04294B
Citation: Dalton Trans., 2019, Advance Article
  • Open access: Creative Commons BY license
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    Monitoring H-cluster assembly using a semi-synthetic HydF protein

    B. Németh, C. Esmieu, H. J. Redman and G. Berggren, Dalton Trans., 2019, Advance Article , DOI: 10.1039/C8DT04294B

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