Evidence map›Paper›PMID 35278753›Full record

ArticleJournal of inorganic biochemistry2022

Visualizing the gas channel of a monofunctional carbon monoxide dehydrogenase.

Alison Biester, Sébastien Dementin, Catherine L Drennan

Open access · hybridAbstract read
In one paragraph

Article in Journal of inorganic biochemistry, 2022. 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
1.6field-weighted citation impact, top 17% 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, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. A Perspective on the Applications of Triphasic Gas Storage in Electrochemical Systems.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  4. Capturing a methanogenic carbon monoxide dehydrogenase/acetyl-CoA synthase complex via cryogenic electron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Review
  6. Article
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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

3 authors at 2 institutions in 3 countries.

Alison BiesterDept. of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, United States.
Sébastien DementinCNRS, Aix-Marseille Université, Laboratoire de Bioénergétique et Ingénierie des Protéines, Institut de Microbiologie de la Méditerranée, 13009 Marseille, France.
Catherine L DrennanDept. of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, United States; Dept. of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, United States; Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139, United States; Canadian Institute for Advanced Research, Bio-inspired Solar Energy Program, Toronto, ON M5G 1M1, Canada. Electronic address: cdrennan@mit.edu.
Massachusetts Institute of Technology · USBioénergétique et Ingénierie des Protéines · FR

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Metalloenzyme structure, function and assemblyR35GM126982 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI CATHERINE L DRENNAN · 2018 to 2026
$3.4M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
Howard Hughes Medical InstituteNCRR NIH HHS S10 RR029205NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R35 GM126982
6 · The paper itself

Abstract

Carbon monoxide dehydrogenase (CODH) plays an important role in the processing of the one‑carbon gases carbon monoxide and carbon dioxide. In CODH enzymes, these gases are channeled to and from the Ni-Fe-S active sites using hydrophobic cavities. In this work, we investigate these gas channels in a monofunctional CODH from Desulfovibrio vulgaris, which is unusual among CODHs for its oxygen-tolerance. By pressurizing D. vulgaris CODH protein crystals with xenon and solving the structure to 2.10 Å resolution, we identify 12 xenon sites per CODH monomer, thereby elucidating hydrophobic gas channels. We find that D. vulgaris CODH has one gas channel that has not been experimentally validated previously in a CODH, and a second channel that is shared with Moorella thermoacetica carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS). This experimental visualization of D. vulgaris CODH gas channels lays groundwork for further exploration of factors contributing to oxygen-tolerance in this CODH, as well as study of channels in other CODHs. We dedicate this publication to the memory of Dick Holm, whose early studies of the Ni-Fe-S clusters of CODH inspired us all.

Indexed as

Aldehyde OxidoreductasesCarbon MonoxideMultienzyme ComplexesOxygenXenonAldehyde OxidoreductasesCarbon Monoxidecarbon monoxide dehydrogenaseMultienzyme ComplexesOxygenXenonCarbon monoxideCO-dehydrogenaseCrystallographyGas channelsTunnelsXenon

Identifiers

PMID35278753
PMCPMC9093221
OpenAlexW4212857681

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.