4.8 Review

[FeFe]-Hydrogenase In Vitro Maturation

Journal

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 61, Issue 49, Pages -

Publisher

WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202212074

Keywords

Biosynthesis; [FeFe]-Hydrogenase; Maturation; Radical SAM; Semisynthetic

Funding

  1. U.S. DOE [DE-SC0005404]
  2. U.S. Department of Energy (DOE) [DE-SC0005404] Funding Source: U.S. Department of Energy (DOE)

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The assembly and installation of the [FeFe]-hydrogenase H-cluster is not fully understood, but in vitro approaches using semisynthetic and enzyme-based methods have provided new insights into the maturation process. These approaches have shed light on the roles of individual maturation enzymes, the nature of H-cluster assembly intermediates, the molecular precursors of H-cluster ligands, and the sequence of steps involved in [FeFe]-hydrogenase maturation.
The [FeFe]-hydrogenase H-cluster is a complex organometallic cofactor whose assembly and installation requires three dedicated accessory proteins referred to as HydE, HydF, and HydG. The roles of these maturases and the precise mechanisms by which they synthesize and insert the H-cluster are not fully understood. This Minireview will focus on new insights into the [FeFe]-hydrogenase maturation process that have been provided by in vitro approaches in which the biosynthetic pathway has been partially or fully reconstructed using semisynthetic and enzyme-based approaches. Specifically, the application of these in vitro, semisynthetic, and fully defined approaches has shed light on the roles of individual maturation enzymes, the nature of H-cluster assembly intermediates, the molecular precursors of H-cluster ligands, and the sequence of steps involved in [FeFe]-hydrogenase maturation.

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