Hydrogenases

Lubitz, Wolfgang; Ogata, Hideaki; Rüdiger, Olaf; Reijerse, Edward J.

doi:10.1021/cr4005814

Cited by 1,835 publications

(2,333 citation statements)

References 639 publications

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“…Most studies on microbial H 2 metabolism focus on only a few branches of the hydrogenase phylogenetic tree and a small subset of organisms within the universal tree of life. Physiological and biochemical characterisations have focussed on model organisms from within five phyla, Proteobacteria, Firmicutes, Cyanobacteria, Euryarchaeota and Chlorophyta (Schwartz et al, 2013;Lubitz et al, 2014). Furthermore, detailed biochemical information and atomicresolution structures are available for only a subset of hydrogenases (Volbeda et al, 1995;Peters et al, 1998;Shima et al, 2008;Fritsch et al, 2011;Mills et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

Genomic and metagenomic surveys of hydrogenase distribution indicate H2 is a widely utilised energy source for microbial growth and survival

et al. 2015

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Recent physiological and ecological studies have challenged the long-held belief that microbial metabolism of molecular hydrogen (H 2 ) is a niche process. To gain a broader insight into the importance of microbial H 2 metabolism, we comprehensively surveyed the genomic and metagenomic distribution of hydrogenases, the reversible enzymes that catalyse the oxidation and evolution of H 2 . The protein sequences of 3286 non-redundant putative hydrogenases were curated from publicly available databases. These metalloenzymes were classified into multiple groups based on (1) amino acid sequence phylogeny, (2) metal-binding motifs, (3) predicted genetic organisation and (4) reported biochemical characteristics. Four groups (22 subgroups) of [NiFe]-hydrogenase, three groups (6 subtypes) of [FeFe]-hydrogenases and a small group of [Fe]-hydrogenases were identified. We predict that this hydrogenase diversity supports H 2 -based respiration, fermentation and carbon fixation processes in both oxic and anoxic environments, in addition to various H 2 -sensing, electron-bifurcation and energy-conversion mechanisms. Hydrogenase-encoding genes were identified in 51 bacterial and archaeal phyla, suggesting strong pressure for both vertical and lateral acquisition. Furthermore, hydrogenase genes could be recovered from diverse terrestrial, aquatic and host-associated metagenomes in varying proportions, indicating a broad ecological distribution and utilisation. Oxygen content (pO 2 ) appears to be a central factor driving the phylum-and ecosystem-level distribution of these genes. In addition to compounding evidence that H 2 was the first electron donor for life, our analysis suggests that the great diversification of hydrogenases has enabled H 2 metabolism to sustain the growth or survival of microorganisms in a wide range of ecosystems to the present day. This work also provides a comprehensive expanded system for classifying hydrogenases and identifies new prospects for investigating H 2 metabolism.

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Section: Introductionmentioning

confidence: 99%

Genomic and metagenomic surveys of hydrogenase distribution indicate H2 is a widely utilised energy source for microbial growth and survival

et al. 2015

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“…These have been focused on silylenes,9 or cyclopentadienyl or arene (half)sandwich systems;10, 11, 12, 13 in these compounds protonation and proton‐coupled electron transfer are of limited relevance to the key chemical reactions of the metal complexes. In contrast, the spectroscopic data we have so obtained can be modelled by ab initio DFT calculations and we show that this provides compelling evidence for the muono‐formyl Fe‐C(Mu)=O and bridging Fe‐Mu‐Fe or terminal Fe‐Mu muonide transients, light isotopes of paramagnetic species that are implicit in hydrogen evolution and uptake 1, 2, 3, 14…”

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confidence: 88%

“…On a per catalytic site basis, the turnover frequencies of certain of these enzymes immobilized on electrodes can rival the best conventional electrocatalyst, carbon‐supported platinum 1, 2, 3. However, the high molecular mass and large geometric footprint of the native enzymes result in rather low current densities, at best ca.…”

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confidence: 99%

Muonium Chemistry at Diiron Subsite Analogues of [FeFe]‐Hydrogenase

et al. 2016

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The chemistry of metal hydrides is implicated in a range of catalytic processes at metal centers. Gaining insight into the formation of such sites by protonation and/or electronation is therefore of significant value in fully exploiting the potential of such systems. Here, we show that the muonium radical (Mu.), used as a low isotopic mass analogue of hydrogen, can be exploited to probe the early stages of hydride formation at metal centers. Mu. undergoes the same chemical reactions as H. and can be directly observed due to its short lifetime (in the microseconds) and unique breakdown signature. By implanting Mu. into three models of the [FeFe]‐hydrogenase active site we have been able to detect key muoniated intermediates of direct relevance to the hydride chemistry of these systems.

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“…HydF has been proposed to function as a template or scaffold for the assembly of the [2Fe] subcluster, which is then transferred as a unit to HydA [1,2]. The only crystal structure of HydF (Figure 4b) was obtained under aerobic conditions and therefore lacks Fe-S clusters.…”

Section: Hydf As a Scaffold For Hyda Maturationmentioning

confidence: 99%

“…The reversible reduction of protons to yield hydrogen is efficiently catalyzed by [FeFe]-hydrogenases [1]. At the core of this catalytic activity is a cofactor, the H-cluster, an organometallic center made up of two subclusters.…”

Section: Introductionmentioning

confidence: 99%

Metallocofactor assembly for [FeFe]-hydrogenases

Dinis

Wieckowski

Roach

2016

Current Opinion in Structural Biology

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Hydrogenases are a potential source of environmentally benign bioenergy, using complex cofactors to catalyze the reversible reduction of protons to form hydrogen. AddressesChemistry and the Institute for Life Sciences, University of Southampton, Highfield Campus, Southampton SO17 1BJ, UK.Corresponding author: Peter L. Roach (plr2@soton.ac.uk). AbstractHydrogenases are a potential source of environmentally benign bioenergy, using complex cofactors to catalyze the reversible reduction of protons to form hydrogen. The most active subclass, the [FeFe]-hydrogenases, is dependent on a metallocofactor, the H cluster, that consists of a two iron subcluster ([2Fe] H ) bridging to a classical cubane cluster ([4Fe-4S] H ). The ligands coordinating to the diiron subcluster include an azadithiolate, three carbon monoxides, and two cyanides. To assemble this complex cofactor, three maturase enzymes, HydG, HydE and HydF are required. The biosynthesis of the diatomic ligands proceeds by an unusual fragmentation mechanism, and structural studies in combination with spectroscopic analysis have started to provide insights into the HydG mediated assembly of a [2Fe] H subcluster precursor.

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Hydrogenases

Cited by 1,835 publications

References 639 publications

Genomic and metagenomic surveys of hydrogenase distribution indicate H2 is a widely utilised energy source for microbial growth and survival

Genomic and metagenomic surveys of hydrogenase distribution indicate H2 is a widely utilised energy source for microbial growth and survival

Muonium Chemistry at Diiron Subsite Analogues of [FeFe]‐Hydrogenase

Metallocofactor assembly for [FeFe]-hydrogenases

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