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Cited by 32Electrochemical sensors and biosensorsEnzyme Catalysis and ImmobilizationElectrocatalysts for Energy Conversion

Bacterial Respiratory Chain Diversity Reveals a Cytochrome c Oxidase Reducing O2 at Low Overpotentials

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Wang, Xie, Clément, Romain, Roger, Magali, Bauzan, Marielle, Mazurenko, Ievgen, Poulpiquet, Anne de, Ilbert, Marianne, Lojou, Elisabeth·2019·Journal of the American Chemical Society
DOI 10.1021/jacs.9b03268
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Abstract

Cytochrome c oxidases (C c Os) are the terminal enzymes in energy-converting chains of microorganisms, where they reduce oxygen into water. Their affinity for O 2 makes them attractive biocatalysts for technological devices in which O 2 concentration is limited, but the high overpotentials they display on electrodes severely limit their applicative use. Here, the C c O of the acidophilic bacterium Acidithiobacillus ferrooxidans is studied on various carbon materials by direct protein electrochemistry and mediated one with redox mediators either diffusing or co-immobilized at the electrode surface. The entrapment of the C c O in a network of hydrophobic carbon nanofibers permits a direct electrochemical communication between the enzyme and the electrode. We demonstrate that the C c O displays a μM affinity for O 2 and reduces O 2 at exceptionally high electrode potentials in the range of +700 to +540 mV vs NHE over a pH range of 4–6. The kinetics of interactions between the enzyme and its physiological partners are fully quantified. Based on these results, an electron transfer pathway allowing O 2 reduction in the acidic metabolic chain is proposed.

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  • The TMPD method is not selective to E. coli bacteria because numerous cells have cytochrome c oxidases in their outer membrane.

    “However, this method is not selective to E. coli bacteria because numerous cells have cytochrome c oxidases in their outer membrane [38].”

    From Trends in single-impact electrochemistry for bacteria analysis (2023) · cites this paper as [38]

    The Introduction (page unavailable) says cytochrome c oxidases are widely distributed among prokaryotes and eukaryotes, supporting the point that they occur in many cells. It does not address the selectivity of a TMPD method or say that these oxidases are in those cells’ outer membranes. (LLM, conf=0.83)

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Authors
Wang, X., Clément, R., Roger, M., Bauzan, M., Mazurenko, I., Poulpiquet, A. D., Ilbert, M., & Lojou, E.
Affiliations
  • Centre National de la Recherche Scientifique (FR)
  • Newcastle University (GB)
  • Aix-Marseille Univ, CNRS, BIP UMR 7281, 31 Chemin Aiguier, CS 70071, 13402 Marseille Cedex 09, France
ORCID
Venue
Journal of the American Chemical Society
Publisher
American Chemical Society (ACS)
Published
2019-06-19
Volume
141
Issue
28
Pages
11093-11102
ISSN
  • 0002-7863 (ISSN-L)
  • 1520-5126
DOI
10.1021/jacs.9b03268
OpenAlex
W2950686550
Cited by
32
References
1
Citations by year
2026: 2 · 2025: 7 · 2024: 5 · 2023: 5 · 2022: 3 · 2021: 4 · 2020: 5 · 2019: 1
FWCI
1.17
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of the American Chemical Society (publishedVersion)
  • PubMed (publishedVersion)
  • HAL (submittedVersion, other-oa)
Funders
  • Agence Nationale de la Recherche (ENZYMOR-ANR-16-CE05- 0024)
  • Aix-Marseille Universit?
  • R?gion PACA
Topics
  • Physical Sciences › Engineering › Electrical and Electronic Engineering › Electrochemical sensors and biosensors
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Electrocatalysts for Energy Conversion
Keywords
cytochrome c oxidase, oxygen reduction reaction, Acidithiobacillus ferrooxidans, acidophilic bacteria, overpotential, redox mediators, carbon nanofibers, enzyme immobilization, electron transfer pathway, electron transport chain, biocatalysis
MeSH terms
Electron Transport Complex IV, Enzymes, Immobilized, Hydrogen-Ion Concentration, Models, Molecular, Oxygen, Acidithiobacillus

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