Evidence map›Paper›PMID 26405831›Full record

ArticleThe ISME journal2016

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

Chris Greening, Ambarish Biswas, Carlo R Carere, Colin J Jackson, Matthew C Taylor, Matthew B Stott, Gregory M Cook, Sergio E Morales

Open access · bronzeAbstract read
In one paragraph

Article in The ISME journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 329 papers.

0numbers the graph read from it
0cells of the map it votes in
329citing papers in PubMed
11.9field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

329 citing papers in PubMed, 677 citations in OpenAlex.

  1. Trial
  2. Redox regulation in OJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
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  3. Article
  4. Electrochemical characterization of C. pasteurianum hydrogenase II and three site-directed variants: catalysis and inhibition.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Article
  5. Genetic dissection of formate hydrogenlyase-2 function: a metalloenzyme involved in bacterial hydrogen production.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
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  17. International journal of systematic and evolutionary microbiology · 2026
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269 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 7 institutions in 2 countries.

Chris GreeningDepartment of Microbiology and Immunology, University of Otago, Dunedin, New Zealand.
Ambarish BiswasDepartment of Microbiology and Immunology, University of Otago, Dunedin, New Zealand.
Carlo R CarereGNS Science, Wairakei Research Centre, Taupō, New Zealand.
Colin J JacksonAustralian National University, Research School of Chemistry, Acton, Australian Capital Territory, Australia.
Matthew C TaylorThe Commonwealth Scientific and Industrial Research Organisation, Land and Water Flagship, Acton, Australian Capital Territory, Australia.
Matthew B StottGNS Science, Wairakei Research Centre, Taupō, New Zealand.
Gregory M CookDepartment of Microbiology and Immunology, University of Otago, Dunedin, New Zealand.
Sergio E MoralesDepartment of Microbiology and Immunology, University of Otago, Dunedin, New Zealand.
University of Otago · NZACT GovernmentAustralian National University · AUCommonwealth Scientific and Industrial Research Organisation · AUGNS Science · NZMaurice Wilkins Centre · NZMuseum of New Zealand Te Papa Tongarewa · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recent physiological and ecological studies have challenged the long-held belief that microbial metabolism of molecular hydrogen (H2) is a niche process. To gain a broader insight into the importance of microbial H2 metabolism, we comprehensively surveyed the genomic and metagenomic distribution of hydrogenases, the reversible enzymes that catalyse the oxidation and evolution of H2. 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 H2-based respiration, fermentation and carbon fixation processes in both oxic and anoxic environments, in addition to various H2-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 (pO2) appears to be a central factor driving the phylum- and ecosystem-level distribution of these genes. In addition to compounding evidence that H2 was the first electron donor for life, our analysis suggests that the great diversification of hydrogenases has enabled H2 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 H2 metabolism.

Indexed as

Amino Acid MotifsArchaeaArchaeal ProteinsBacteriaBacterial ProteinsEcosystemGenomicsHydrogenHydrogenaseMetagenomicsOxidation-ReductionPhylogenyArchaeal ProteinsBacterial ProteinsHydrogenHydrogenase

Identifiers

PMID26405831
PMCPMC4817680
OpenAlexW1873911178

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.