Malmö University Publications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Octaheme nitrite reductase: The mechanism of intramolecular electron transfer and kinetics of nitrite bioelectroreduction.
Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV).
Malmö University, Faculty of Health and Society (HS), Department of Biomedical Science (BMV). Malmö University, Biofilms Research Center for Biointerfaces. Research Centre of Biotechnology, Russian Academy of Sciences, 119071 Moscow, Russia.ORCID iD: 0000-0001-6421-2158
Research Centre of Biotechnology, Russian Academy of Sciences, 119071 Moscow, Russia.
Research Centre of Biotechnology, Russian Academy of Sciences, 119071 Moscow, Russia.
Show others and affiliations
2021 (English)In: Bioelectrochemistry, ISSN 1567-5394, E-ISSN 1878-562X, Vol. 138, article id 107699Article in journal (Refereed) Published
Abstract [en]

Detailed impedance and voltammetric studies of hexameric octaheme nitrite reductase immobilized on carbon-based nanomaterials, specifically nanotubes and nanoparticles, were performed. Well-pronounced bioelectrocatalytic reduction of nitrite on enzyme-modified electrodes was obtained. Analysis of the impedance data indicated the absence of long-lived intermediates involved in the nitrite reduction. Cyclic voltammograms of biomodified electrodes had a bi-sigmoidal shape, which pointed to the presence of two enzyme orientations on carbon supports. The maximum (limiting) catalytic currents were determined and, by applying the correction by the mixed kinetics equation, the Tafel dependences were plotted for each catalytic wave/each enzyme orientation. Finally, two schemes for the rate-limiting processes during bioelectrocatalysis were proposed, viz. for low- and high-potential orientations.

Place, publisher, year, edition, pages
Elsevier, 2021. Vol. 138, article id 107699
Keywords [en]
Bioelectrocatalysis, Intramolecular electron transfer, Octaheme nitrite reductase, Thioalkalivibrio paradoxus
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:mau:diva-37406DOI: 10.1016/j.bioelechem.2020.107699ISI: 000663533800011PubMedID: 33221569Scopus ID: 2-s2.0-85096713287OAI: oai:DiVA.org:mau-37406DiVA, id: diva2:1507828
Available from: 2020-12-08 Created: 2020-12-08 Last updated: 2023-10-31Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textPubMedScopus

Authority records

Andoralov, VictorShleev, Sergey

Search in DiVA

By author/editor
Andoralov, VictorShleev, Sergey
By organisation
Department of Biomedical Science (BMV)Biofilms Research Center for Biointerfaces
In the same journal
Bioelectrochemistry
Medical and Health Sciences

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 66 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf