English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Preliminary electrochemical studies of the flavohaemoprotein from Ralstonia eutropha entrapped in a film of methyl cellulose: activation of the reduction of dioxygen

de Olivereira, P., Ranjbari, A., Baciou, L., Bizouarn, T., Ollesch, G., Ermler, U., et al. (2007). Preliminary electrochemical studies of the flavohaemoprotein from Ralstonia eutropha entrapped in a film of methyl cellulose: activation of the reduction of dioxygen. Bioelectrochemistry, 70(1), 185-191. doi:10.1016/j.bioelechem.2006.03.018.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
de Olivereira, Pedro1, Author
Ranjbari, Alireza1, Author
Baciou, Laura1, Author
Bizouarn, Tania1, Author
Ollesch, Gabriella2, Author              
Ermler, Ulrich2, Author              
Sebban, Pierre1, Author
Keita, Bineta1, Author
Nadjo, Louis1, Author
Affiliations:
1Laboratoire de Chimie Physique, UMR 8000 CNRS, Faculté des Sciences d'Orsay Université Paris-Sud XI, Bât 350, 15 rue Georges Clemenceau, 91405 Orsay Cedex, France, ou_persistent22              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

Content

show
hide
Free keywords: Flavohaemoprotein; Cyclic voltammetry; Methyl cellulose; Spectroelectrochemistry; Chronocoulometry; Dioxygen reduction activation
 Abstract: A flavohaemoprotein (FHP) from Ralstonia eutropha, obtained in a pure and active form, has been entrapped in a film of methyl cellulose on the electrode surface and gives a stable and reproducible electrochemical response at pH 7.00 when subject to cyclic voltammetry using a glassy carbon electrode. To our knowledge, no previous direct electrochemistry had been achieved with a bacterial flavohaemoglobin, which possess both a FAD and a haem. A single couple is observed which is assigned to the haem moiety of the protein, since the same result is obtained with a semi-apo form of the protein deprived of FAD (semi-apo FHP). The data collected were further confirmed by potentiometry with a platinum electrode, and the homogeneous electron transfer rate estimated by double potential step chronocoulometry at a bare glassy carbon electrode in the presence of methyl viologen (MV). The presence of FAD in the holoprotein is easily confirmed by UV–Vis spectrophotometry, but its expected electron relay role remains elusive. The protein activates the reduction of dioxygen by about 400 mV, the reduction current being proportional to the concentration of dioxygen up to 10% in volume in the gas mixture.

Details

show
hide
Language(s): eng - English
 Dates: 2005-06-022006-04-052007-01-01
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.bioelechem.2006.03.018
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Bioelectrochemistry
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Elsevier B.V.
Pages: - Volume / Issue: 70 (1) Sequence Number: - Start / End Page: 185 - 191 Identifier: ISSN: 1567-5394
CoNE: https://pure.mpg.de/cone/journals/resource/1567-5394