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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Role of ammonia-lyases in the synthesis of the dithiomethylamine ligand during [FeFe]-hydrogenase maturation.
J Biol Chem
October 2024
Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana, USA. Electronic address:
The generation of an active [FeFe]-hydrogenase requires the synthesis of a complex metal center, the H-cluster, by three dedicated maturases: the radical S-adenosyl-l-methionine (SAM) enzymes HydE and HydG, and the GTPase HydF. A key step of [FeFe]-hydrogenase maturation is the synthesis of the dithiomethylamine (DTMA) bridging ligand, a process recently shown to involve the aminomethyl-lipoyl-H-protein from the glycine cleavage system, whose methylamine group originates from serine and ammonium. Here we use functional assays together with electron paramagnetic resonance and electron-nuclear double resonance spectroscopies to show that serine or aspartate together with their respective ammonia-lyase enzymes can provide the nitrogen for DTMA biosynthesis during in vitro [FeFe]-hydrogenase maturation.
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Acc Chem Res
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Department of Chemistry, University of California, Davis, Davis, California 95616, United States.
ConspectusNature's prototypical hydrogen-forming catalysts─hydrogenases─have attracted much attention because they catalyze hydrogen evolution at near zero overpotential and ambient conditions. Beyond any possible applications in the energy sphere, the hydrogenases feature complicated active sites, which implies novel biosynthetic pathways. In terms of the variety of cofactors, the [FeFe]-hydrogenase is among the most complex.
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School of Chemical Sciences, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
The paper aims to elucidate the final stages in the biosynthesis of the [2Fe] active site of the [FeFe]-hydrogenases. The recently hypothesized intermediate [Fe(SCHNH)(CN)(CO)] ([1]) was prepared by a multistep route from [Fe(S)(CN)(CO)]. The following synthetic intermediates were characterized in order: [Fe(SCHNHFmoc)(CNBEt)(CO)], [Fe(SCHNHFmoc)(CN)-(CO)], and [Fe(SCHNHFmoc)(CN)(CO)], where Fmoc is fluorenylmethoxycarbonyl).
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Angew Chem Int Ed Engl
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Univ. Grenoble-Alpes, CEA, CNRS, IBS, Metalloproteins Unit, 38000, Grenoble, France.
[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.
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Department of Chemistry, University of California, Davis, Davis, California 95616, United States.
[FeFe] hydrogenases contain a 6-Fe cofactor that serves as the active site for efficient redox interconversion between H and protons. The biosynthesis of the so-called H-cluster involves unusual enzymatic reactions that synthesize organometallic Fe complexes containing azadithiolate, CO, and CN ligands. We have previously demonstrated that specific synthetic [Fe(CO)(CN)] complexes can be used to functionally replace proposed Fe intermediates in the maturation reaction.
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