Redox potentials of the blue copper sites of bilirubin oxidases
(2006) In Biochimica et Biophysica Acta - Bioenergetics 1757(12). p.1634-1641- Abstract
- The redox potentials of the multicopper redox enzyme bilirubin oxidase (BOD) from two organisms were determined by mediated and direct spectroelectrochemistry. The potential of the T1 site of BOD from the fungus Myrothecium verrucaria was close to 670 mV, whereas that from Trachyderma tsunodae was > 650 mV vs. NHE. For the first time, direct electron transfer was observed between gold electrodes and BODs. The redox potentials of the T2 sites of both BODs were near 390 mV vs. NHE, consistent with previous finding for laccase and suggesting that the redox potentials of the T2 copper sites of most blue multicopper oxidases are similar, about 400 mV (c) 2006 Elsevier B.V. All rights reserved.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/680415
- author
- Christenson, Andreas LU ; Shleev, Sergey LU ; Mano, Nicolas ; Heller, Adam and Gorton, Lo LU
- organization
- publishing date
- 2006
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- redox titration, T3 sites, T2, T1, redox potential, bilirubin oxidase, copper enzyme, spectroelectrochemistry
- in
- Biochimica et Biophysica Acta - Bioenergetics
- volume
- 1757
- issue
- 12
- pages
- 1634 - 1641
- publisher
- Elsevier
- external identifiers
-
- wos:000243154000011
- scopus:33751533743
- ISSN
- 0005-2728
- DOI
- 10.1016/j.bbabio.2006.08.008
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Analytical Chemistry (S/LTH) (011001004)
- id
- fc87f6ed-26b4-4768-b785-417637b0286e (old id 680415)
- date added to LUP
- 2016-04-01 16:43:09
- date last changed
- 2022-03-07 07:53:08
@article{fc87f6ed-26b4-4768-b785-417637b0286e, abstract = {{The redox potentials of the multicopper redox enzyme bilirubin oxidase (BOD) from two organisms were determined by mediated and direct spectroelectrochemistry. The potential of the T1 site of BOD from the fungus Myrothecium verrucaria was close to 670 mV, whereas that from Trachyderma tsunodae was > 650 mV vs. NHE. For the first time, direct electron transfer was observed between gold electrodes and BODs. The redox potentials of the T2 sites of both BODs were near 390 mV vs. NHE, consistent with previous finding for laccase and suggesting that the redox potentials of the T2 copper sites of most blue multicopper oxidases are similar, about 400 mV (c) 2006 Elsevier B.V. All rights reserved.}}, author = {{Christenson, Andreas and Shleev, Sergey and Mano, Nicolas and Heller, Adam and Gorton, Lo}}, issn = {{0005-2728}}, keywords = {{redox titration; T3 sites; T2; T1; redox potential; bilirubin oxidase; copper enzyme; spectroelectrochemistry}}, language = {{eng}}, number = {{12}}, pages = {{1634--1641}}, publisher = {{Elsevier}}, series = {{Biochimica et Biophysica Acta - Bioenergetics}}, title = {{Redox potentials of the blue copper sites of bilirubin oxidases}}, url = {{http://dx.doi.org/10.1016/j.bbabio.2006.08.008}}, doi = {{10.1016/j.bbabio.2006.08.008}}, volume = {{1757}}, year = {{2006}}, }