Evidence map›Paper›PMID 26703931›Full record

ArticleInorganic chemistry2016

Biosynthesis of the [FeFe] Hydrogenase H Cluster: A Central Role for the Radical SAM Enzyme HydG.

Daniel L M Suess, Jon M Kuchenreuther, Liliana De La Paz, James R Swartz, R David Britt

Open access · greenAbstract read
In one paragraph

Article in Inorganic chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

11 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Characterization of Complex-B ([Fe(κJournal of the American Chemical Society · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. The binuclear cluster of [FeFe] hydrogenase is formed with sulfur donated by cysteine of an [Fe(Cys)(CO)Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  7. Enzymatic Cascade Reactions in Biosynthesis.Angewandte Chemie (International ed. in English) · 2019
    Review
  8. Monitoring H-cluster assembly using a semi-synthetic HydF protein.Dalton transactions (Cambridge, England : 2003) · 2019
    Article
  9. Review
  10. Article
  11. Review
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

5 authors at 1 institution in 1 country.

Daniel L M SuessDepartment of Chemistry, University of California, Davis , Davis, California 95616, United States.
Jon M KuchenreutherDepartment of Chemistry, University of California, Davis , Davis, California 95616, United States.
Liliana De La Paz
James R Swartz
R David BrittDepartment of Chemistry, University of California, Davis , Davis, California 95616, United States.
University of California, Davis · US

Funding

Mechanisms of Radical SAM Enzymes Probed by EPR SpectroscopyR01GM104543 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI BRITT, R DAVID · 2014 to 2017
$1.2M
Mechanistic Investigations of [FeFe] Hydrogenase H-Cluster AssemblyF32GM111025 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI SUESS, DANIEL LEIF MIGDOW · 2014 to 2016
$158k
NIGMS NIH HHS F32 GM111025NIGMS NIH HHS F32GM111025NIGMS NIH HHS R01 GM104543NIGMS NIH HHS R01GM104543
6 · The paper itself

Abstract

Hydrogenase enzymes catalyze the rapid and reversible interconversion of H2 with protons and electrons. The active site of the [FeFe] hydrogenase is the H cluster, which consists of a [4Fe-4S]H subcluster linked to an organometallic [2Fe]H subcluster. Understanding the biosynthesis and catalytic mechanism of this structurally unusual active site will aid in the development of synthetic and biological hydrogenase catalysts for applications in solar fuel generation. The [2Fe]H subcluster is synthesized and inserted by three maturase enzymes-HydE, HydF, and HydG-in a complex process that involves inorganic, organometallic, and organic radical chemistry. HydG is a member of the radical S-adenosyl-l-methionine (SAM) family of enzymes and is thought to play a prominent role in [2Fe]H subcluster biosynthesis by converting inorganic Fe(2+), l-cysteine (Cys), and l-tyrosine (Tyr) into an organometallic [(Cys)Fe(CO)2(CN)](-) intermediate that is eventually incorporated into the [2Fe]H subcluster. In this Forum Article, the mechanism of [2Fe]H subcluster biosynthesis is discussed with a focus on how this key [(Cys)Fe(CO)2(CN)](-) species is formed. Particular attention is given to the initial metallocluster composition of HydG, the modes of substrate binding (Fe(2+), Cys, Tyr, and SAM), the mechanism of SAM-mediated Tyr cleavage to CO and CN(-), and the identification of the final organometallic products of the reaction.

Indexed as

Bacterial ProteinsCatalysisElectron Spin Resonance SpectroscopyEscherichia coliHydrogenaseIron-Sulfur ProteinsShewanellaBacterial ProteinsHydrogenaseiron hydrogenaseIron-Sulfur Proteins

Identifiers

PMID26703931
PMCPMC4780679
OpenAlexW2211081036

What OpenQuestion holds

Textmetadata
LicenceTDM
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.