The Electrically Wired Molybdenum Domain of Human Sulfite Oxidase is Bioelectrocatalytically Active
(2015) In European Journal of Inorganic Chemistry p.3526-3531- Abstract
- We report electron transfer between the catalytic molybdenum cofactor (Moco) domain of human sulfite oxidase (hSO) and electrodes through a poly(vinylpyridine)-bound [osmium(N,N'-methyl-2,2'-biimidazole)(3)](2+/3+) complex as the electron-transfer mediator. The biocatalyst was immobilized in this low-potential redox polymer on a carbon electrode. Upon the addition of sulfite to the immobilized separate Moco domain, the generation of a significant catalytic current demonstrated that the catalytic center is effectively wired and active. The bioelectrocatalytic current of the wired separate catalytic domain reached 25% of the signal of the wired full molybdoheme enzyme hSO, in which the heme b(5) is involved in the electron-transfer pathway.... (More)
- We report electron transfer between the catalytic molybdenum cofactor (Moco) domain of human sulfite oxidase (hSO) and electrodes through a poly(vinylpyridine)-bound [osmium(N,N'-methyl-2,2'-biimidazole)(3)](2+/3+) complex as the electron-transfer mediator. The biocatalyst was immobilized in this low-potential redox polymer on a carbon electrode. Upon the addition of sulfite to the immobilized separate Moco domain, the generation of a significant catalytic current demonstrated that the catalytic center is effectively wired and active. The bioelectrocatalytic current of the wired separate catalytic domain reached 25% of the signal of the wired full molybdoheme enzyme hSO, in which the heme b(5) is involved in the electron-transfer pathway. This is the first report on a catalytically active wired molybdenum cofactor domain. The formal potential of this electrochemical mediator is between the potentials of the two cofactors of hSO, and as hSO can occupy several conformations in the polymer matrix, it is imaginable that electron transfer from the catalytic site to the electrode through the osmium center occurs for the hSO molecules in which the Moco domain is sufficiently accessible. The observation of catalytic oxidation currents at low potentials is favorable for applications in bioelectronic devices. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/7975545
- author
- Spricigo, Roberto ; Leimkuehler, Silke ; Gorton, Lo LU ; Scheller, Frieder W. and Wollenberger, Ulla
- organization
- publishing date
- 2015
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Metalloenzymes, Enzyme catalysis, Immobilization, Osmium
- in
- European Journal of Inorganic Chemistry
- issue
- 21
- pages
- 3526 - 3531
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- wos:000359297800017
- scopus:84938206331
- ISSN
- 1099-0682
- DOI
- 10.1002/ejic.201500034
- language
- English
- LU publication?
- yes
- id
- 3f0602b1-1a45-4483-86b3-1b1878800d75 (old id 7975545)
- date added to LUP
- 2016-04-01 10:49:46
- date last changed
- 2022-03-12 17:28:29
@article{3f0602b1-1a45-4483-86b3-1b1878800d75,
abstract = {{We report electron transfer between the catalytic molybdenum cofactor (Moco) domain of human sulfite oxidase (hSO) and electrodes through a poly(vinylpyridine)-bound [osmium(N,N'-methyl-2,2'-biimidazole)(3)](2+/3+) complex as the electron-transfer mediator. The biocatalyst was immobilized in this low-potential redox polymer on a carbon electrode. Upon the addition of sulfite to the immobilized separate Moco domain, the generation of a significant catalytic current demonstrated that the catalytic center is effectively wired and active. The bioelectrocatalytic current of the wired separate catalytic domain reached 25% of the signal of the wired full molybdoheme enzyme hSO, in which the heme b(5) is involved in the electron-transfer pathway. This is the first report on a catalytically active wired molybdenum cofactor domain. The formal potential of this electrochemical mediator is between the potentials of the two cofactors of hSO, and as hSO can occupy several conformations in the polymer matrix, it is imaginable that electron transfer from the catalytic site to the electrode through the osmium center occurs for the hSO molecules in which the Moco domain is sufficiently accessible. The observation of catalytic oxidation currents at low potentials is favorable for applications in bioelectronic devices.}},
author = {{Spricigo, Roberto and Leimkuehler, Silke and Gorton, Lo and Scheller, Frieder W. and Wollenberger, Ulla}},
issn = {{1099-0682}},
keywords = {{Metalloenzymes; Enzyme catalysis; Immobilization; Osmium}},
language = {{eng}},
number = {{21}},
pages = {{3526--3531}},
publisher = {{John Wiley & Sons Inc.}},
series = {{European Journal of Inorganic Chemistry}},
title = {{The Electrically Wired Molybdenum Domain of Human Sulfite Oxidase is Bioelectrocatalytically Active}},
url = {{http://dx.doi.org/10.1002/ejic.201500034}},
doi = {{10.1002/ejic.201500034}},
year = {{2015}},
}