Publikationer från Malmö universitet
Ändra sökning
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Direct heterogeneous electron transfer reactions of Bacillus halodurans bacterial blue multicopper oxidase
Malmö högskola, Fakulteten för hälsa och samhälle (HS). Laboratory of Chemical Enzymology, A. N. Bach Institute of Biochemistry, Russian Academy of Sciences 119071 Moscow, Russia; Department of Analytical Chemistry, Lund University, SE-221 00 Lund, Sweden.ORCID-id: 0000-0001-6421-2158
Science Research Centre, Science Park, Harbin Institute of Technology, 150001 Harbin, P. R. China.
Department of Analytical Chemistry, Lund University, SE-221 00 Lund, Sweden.
Laboratory of Chemical Enzymology, A. N. Bach Institute of Biochemistry, Russian Academy of Sciences 119071 Moscow, Russia.
Visa övriga samt affilieringar
2008 (Engelska)Ingår i: Electroanalysis, ISSN 1040-0397, E-ISSN 1521-4109, Vol. 20, nr 9, s. 963-969Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Direct electron transfer reactions of Bacillus halodurans bacterial multicopper oxidase on bare spectrographic graphite, as well as bare and thiol-modified gold electrodes were studied using cyclic voltammetry, potentiometry, amperometry, and spectroelectrochemistry. The redox potential of the T1 site of the enzyme was measured using mediatorless redox titration and found to be 325 mV±10 mV vs. NHE. From measurements with a mercaptopropionic acid-modified gold electrode under aerobic conditions a midpoint potential of 360 mV vs. NHE for the T2/T3 copper cluster is deduced. Differing from most other characterized laccases of fungal and plant origins this bacterial enzyme exhibits bioelectrocatalytic activity at neutral pH and tolerates high chloride concentrations (200 mM), conditions that usually strongly inhibit catalysis. Moreover, it has the very high affinity towards molecular oxygen both in solution and in the adsorbed state (KM≤50 μM).

Ort, förlag, år, upplaga, sidor
John Wiley & Sons, 2008. Vol. 20, nr 9, s. 963-969
Nationell ämneskategori
Analytisk kemi
Identifikatorer
URN: urn:nbn:se:mau:diva-15264DOI: 10.1002/elan.200704116ISI: 000255770800005Scopus ID: 2-s2.0-54549122413Lokalt ID: 6930OAI: oai:DiVA.org:mau-15264DiVA, id: diva2:1418785
Tillgänglig från: 2020-03-30 Skapad: 2020-03-30 Senast uppdaterad: 2024-05-06Bibliografiskt granskad

Open Access i DiVA

Fulltext saknas i DiVA

Övriga länkar

Förlagets fulltextScopus

Person

Shleev, SergeyRuzgas, Tautgirdas

Sök vidare i DiVA

Av författaren/redaktören
Shleev, SergeyRuzgas, Tautgirdas
Av organisationen
Fakulteten för hälsa och samhälle (HS)
I samma tidskrift
Electroanalysis
Analytisk kemi

Sök vidare utanför DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetricpoäng

doi
urn-nbn
Totalt: 16 träffar
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf