The Redox Environment in the Mitochondrial Intermembrane Space Is Maintained Separately from the Cytosol and Matrix
Open accessAbstract
Redox control in the mitochondrion is essential for the proper functioning of this organelle. Disruption of mitochondrial redox processes contributes to a host of human disorders, including cancer, neurodegenerative diseases, and aging. To better characterize redox control pathways in this organelle, we have targeted a green fluorescent protein-based redox sensor to the intermembrane space (IMS) and matrix of yeast mitochondria. This approach allows us to separately monitor the redox state of the matrix and the IMS, providing a more detailed picture of redox processes in these two compartments. To verify that the sensors respond to localized glutathione (GSH) redox changes, we have genetically manipulated the subcellular redox state using oxidized GSH (GSSG) reductase localization mutants. These studies indicate that redox control in the cytosol and matrix are maintained separately by cytosolic and mitochondrial isoforms of GSSG reductase. Our studies also demonstrate that the mitochondrial IMS is considerably more oxidizing than the cytosol and mitochondrial matrix and is not directly influenced by endogenous GSSG reductase activity. These redox measurements are used to predict the oxidation state of thiol-containing proteins that are imported into the IMS.
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Protein-based redox probes have drawbacks due, in part, to their reliance on cellular Grxs and their lag-time to equilibrate with cellular GSSG.
“Despite the advantage of the real-time values that can be tracked by these intracellular sensors, there may be other drawbacks of these protein-based probes due, in part, on their reliance on cellular Grxs and their lag-time to equilibrate with cellular GSSG (178, 319).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [178]
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References 57 · Cited by 273
Research works printed but not linked: 2
- Holmgren, A., Johansson, C., Berndt, C., Lonn, M. E., Hudemann, C., and Lillig, C. H. (2005) Biochem. Soc. Trans. 33, 1375-1377
- Mårtensson, J., Lai, J. C., and Meister, A. (1990) Proc. Natl. Acad. Sci.
- Authors
- Hu, J., Dong, L., & Outten, C. E.
- Affiliations
- University of South Carolina (US)
- Corresponding author
- Outten, Caryn E.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2008-10
- Volume
- 283
- Issue
- 43
- Pages
- 29126-29134
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2570890
- OpenAlex
- W2000523097
- Cited by
- 273
- References
- 57
- Citations by year
- 2026: 11 · 2025: 10 · 2024: 9 · 2023: 9 · 2022: 8 · 2021: 15 · 2020: 13 · 2019: 13 · 2018: 13 · 2017: 21 · 2016: 26 · 2015: 11 · 2014: 21 · 2013: 17 · 2012: 21
- FWCI
- 7.41
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Scholar Commons (University of South Carolina) (submittedVersion)
- Funders
- Johns Hopkins University
- University of South Carolina
- National Institutes of Health
- National Institute of Environmental Health Sciences (ES13780, K22ES013780)
- 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 › Biochemistry › Sulfur Compounds in Biology
- Keywords
- mitochondrial redox state, mitochondrial intermembrane space, mitochondrial matrix, GSSG reductase, redox sensors, yeast mitochondria
- MeSH terms
- Bacterial Proteins, Cytosol, Extracellular Matrix, Glutathione, Humans, Hydrogen-Ion Concentration, Luminescent Proteins, Microscopy, Fluorescence, Mitochondria, Models, Biological, Mutation, Oxidation-Reduction, Oxygen, Saccharomyces cerevisiae, Subcellular Fractions, Oxidants
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