Evidence map›Paper›PMID 24147852›Full record

ArticleJournal of the American Chemical Society2013

(13)C and (63,65)Cu ENDOR studies of CO dehydrogenase from Oligotropha carboxidovorans. Experimental evidence in support of a copper-carbonyl intermediate.

Muralidharan Shanmugam, Jarett Wilcoxen, Diana Habel-Rodriguez, George E Cutsail, Martin L Kirk, Brian M Hoffman, Russ Hille

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Magnetic interactions between metal sites in complex enzymes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025
    Review
  3. Insights into periplasmic nitrate reductase function under single turnover.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Article
  4. Article
  5. Review
  6. Review
  7. Can Water Act as a Nucleophile in CO Oxidation Catalysed by Mo/Cu CO-Dehydrogenase? Answers from Theory.Chemphyschem : a European journal of chemical physics and physical chemistry · 2022
    Article
  8. Article
  9. Article
  10. The ChallengingFrontiers in chemistry · 2018
    Review
  11. A realistic in silico model for structure/function studies of molybdenum-copper CO dehydrogenase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016
    Article
  12. The aerobic CO dehydrogenase from Oligotropha carboxidovorans.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015
    Review
  13. Electronic structure contributions to reactivity in xanthine oxidase family enzymes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015
    Review
  14. The mononuclear molybdenum enzymes.Chemical reviews · 2014
    Review
  15. Orbital contributions to CO oxidation in Mo-Cu carbon monoxide dehydrogenase.Chemical communications (Cambridge, England) · 2014
    Article
  16. Article
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

7 authors at 3 institutions in 1 country.

Muralidharan ShanmugamDepartment of Chemistry, Northwestern University , Evanston, Illinois 60208-3113, United States.
Jarett Wilcoxen
Diana Habel-Rodriguez
George E Cutsail
Martin L Kirk
Brian M Hoffman
Russ Hille
Northwestern University · USUniversity of California, Riverside · USUniversity of New Mexico · US

Funding

Spectroscopic Studies of Molybdoenzymes & ModelsR01GM057378 · NIGMS · UNIVERSITY OF NEW MEXICO · PI MARTIN L KIRK · 1998 to 2026
$6.9M
Studies of environmentally relevant molybdenum enzymesR01ES012658 · NIEHS · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI HILLE, RUSS · 2005 to 2009
$1.5M
NIEHS NIH HHS R01 ES012658NIGMS NIH HHS GM 057378NIGMS NIH HHS R01 GM057378
6 · The paper itself

Abstract

We report here an ENDOR study of an S = 1/2 intermediate state trapped during reduction of the binuclear Mo/Cu enzyme CO dehydrogenase by CO. ENDOR spectra of this state confirm that the (63,65)Cu nuclei exhibits strong and almost entirely isotropic coupling to the unpaired electron, show that this coupling atypically has a positive sign, aiso = +148 MHz, and indicate an apparently undetectably small quadrupolar coupling. When the intermediate is generated using (13)CO, coupling to the (13)C is observed, with aiso = +17.3 MHz. A comparison with the couplings seen in related, structurally assigned Mo(V) species from xanthine oxidase, in conjunction with complementary computational studies, leads us to conclude that the intermediate contains a partially reduced Mo(V)/Cu(I) center with CO bound at the copper. Our results provide strong experimental support for a reaction mechanism that proceeds from a comparable complex of CO with fully oxidized Mo(VI)/Cu(I) enzyme.

Indexed as

Aldehyde OxidoreductasesAlphaproteobacteriaCatalytic DomainCopperElectron Spin Resonance SpectroscopyModels, MolecularMultienzyme ComplexesAldehyde Oxidoreductasescarbon monoxide dehydrogenaseCopperMultienzyme Complexes

Identifiers

PMID24147852
PMCPMC4521601
OpenAlexW2322828178

What OpenQuestion holds

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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.