Sökning: id:"swepub:oai:DiVA.org:liu-98797" >
Regeneration of the...
Regeneration of the antioxidant ubiquinol by lipoamide dehydrogenase, thioredoxin reductase and glutathione reductase
-
- Nordman, Tomas (författare)
- Department of Laboratory Medicine, F 46, Karolinska Institutet, Huddinge University Hospital, Stockholm, Sweden
-
- Xia, Ling (författare)
- Department of Laboratory Medicine, F 46, Karolinska Institutet, Huddinge University Hospital, Stockholm, Sweden
-
- Björkhem-Bergman, Linda (författare)
- Karolinska Institutet
-
visa fler...
-
- Damdimopoulos, Anastassios (författare)
- Karolinska Institutet
-
- Nalvarte, Ivan (författare)
- Karolinska Institutet
-
- Arnér, Elias S.J. (författare)
- Karolinska Institutet
-
- Spyrou, Giannis (författare)
- Department of Biosciences at Novum, Center for Biotechnology, Karolinska Institutet, Huddinge, Sweden
-
- Eriksson, Lennart C. (författare)
- Karolinska Institutet
-
- Björnstedt, Mikael (författare)
- Karolinska Institutet
-
- Olsson, Jerker M. (författare)
- Department of Laboratory Medicine, F 46, Karolinska Institutet, Huddinge University Hospital, Stockholm, Sweden
-
visa färre...
-
(creator_code:org_t)
- IOS Press, 2003
- 2003
- Engelska.
-
Ingår i: Biofactors. - : IOS Press. - 0951-6433 .- 1872-8081. ; 18:1-4, s. 45-50
- Relaterad länk:
-
http://iospress.meta...
-
visa fler...
-
https://urn.kb.se/re...
-
http://kipublication...
-
https://doi.org/10.1...
-
visa färre...
Abstract
Ämnesord
Stäng
- Ubiquinol is a powerful antioxidant, which is oxidized in action and needs to be replaced or regenerated to be capable of a sustained effort. This article summarises current knowledge of extramitochondrial reduction of ubiquinone by three flavoenzymes, i.e. lipoamide dehydrogenase, glutathione reductase and thioredoxin reductase, belonging to the same pyridine nucleotide-disulfide oxidoreductase family. These three enzymes are the most efficient extramitochondrial ubiquinone reductases so far described. The reduction of ubiquinone by lipoamide dehydrogenase and glutathione reductase is potently stimulated by zinc and the highest rate of reduction is achieved at acidic pH and the rates are equal with either NADPH or NADH as co-factors. The most efficient ubiquinone reductases are mammalian cytosolic thioredoxin reductases, which are selenoenzymes with a number of biological functions. Reduction of ubiquinone by thioredoxin reductase is in contrast to the other two enzymes investigated, inhibited by zinc and shows a sharp physiological pH optimum at pH 7.5. Furthermore, the reaction is selenium dependent as revealed from experiments using truncated and mutant forms of the enzyme and also in a cellular context by selenium treatment of transfected thioredoxin reductase overexpressing stable cell lines. The reduction of ubiquinone by the three enzymes offers a multifunctional system for extramitochondrial regeneration of an important antioxidant.
Nyckelord
- ubiquinone; lipoamide dehydrogenase; glutathione reductase; thioredoxin reductase; oxidative stress
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas