Purification of Mitochondrial Thioredoxin Reductase and Its Involvement in the Redox Regulation of Membrane Permeability
Open accessAbstract
The isolation to purity of a rat liver mitochondrial thioredoxin reductase is reported. The mitochondrial enzyme shows a chromatographic behavior different from that of the cytosolic enzyme. The purified enzyme, after sodium dodecylsulfate-polyacrylamide gel electrophoresis, yields a single band with a molecular weight of approximately 54 kDa. The apparent Km for E. coli thioredoxin is about 13 microM, while the apparent Km for 5,5'-dithiobis (2-nitrobenzoic acid) is 530 microM, values comparable to those reported for the cytosolic enzyme. Mitochondrial thioredoxin reductase, in addition to its natural substrate thioredoxin, is also able to reduce chemically unrelated compounds such as 5,5 '-dithiobis (2-nitrobenzoic acid), selenite, and alloxan; the enzyme is inhibited by classical inhibitors of the cytosolic enzyme such as 1-chloro-2,4-dinitrobenzene and 13-cis-retinoic acid. A strong inhibitory action is also elicited by Mn2+ and Zn2+ ions. Thiol status appears critically involved in the control of membrane permeability and, therefore, a thiol/disulfide transition involving reduced pyridine nucleotides, matrix soluble thiols, and inner membrane thiols appears to play a fundamental role. The potential role of thioredoxin/thioredoxin reductase system in the control and redox regulation of the mitochondrial membrane permeability, is discussed.
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- Authors
- Rigobello, M. P., Callegaro, M. T., Barzon, E., Benetti, M., & Bindoli, A.
- Affiliations
- University of Padua (IT)
- Corresponding author
- Bindoli, Alberto
- ORCID
- Rigobello, Maria Pia
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 1998-01
- Volume
- 24
- Issue
- 2
- Pages
- 370-376
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W1994977897
- Cited by
- 138
- References
- 34
- Citations by year
- 2024: 1 · 2023: 5 · 2021: 3 · 2020: 2 · 2019: 1 · 2018: 3 · 2017: 3 · 2016: 5 · 2015: 4 · 2014: 8 · 2013: 4 · 2012: 3
- FWCI
- 2.79
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Padua Research Archive (University of Padova) (submittedVersion, other-oa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Aldose Reductase and Taurine
- Keywords
- enzyme purification, thioredoxin, redox regulation, mitochondrial membrane permeability, pyridine nucleotides, selenite reduction, 5,5'-dithiobis(2-nitrobenzoic acid), enzyme inhibitors, metal ion inhibition, rat liver mitochondria
- MeSH terms
- Alloxan, Animals, Calcium, Dinitrochlorobenzene, Dithionitrobenzoic Acid, Electrophoresis, Polyacrylamide Gel, Enzyme Inhibitors, Intracellular Membranes, Manganese, Mitochondria, Liver, Molecular Weight, Oxidation-Reduction, Permeability, Thioredoxin-Disulfide Reductase, Zinc, Isotretinoin, Sodium Selenite, Rats
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