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A role for cytochrome c and cytochrome c peroxidase in electron shuttling from Erv1
Open accessAbstract
Erv1 is a flavin-dependent sulfhydryl oxidase in the mitochondrial intermembrane space (IMS) that functions in the import of cysteine-rich proteins. Redox titrations of recombinant Erv1 showed that it contains three distinct couples with midpoint potentials of -320, -215, and -150 mV. Like all redox-active enzymes, Erv1 requires one or more electron acceptors. We have generated strains with erv1 conditional alleles and employed biochemical and genetic strategies to facilitate identifying redox pathways involving Erv1. Here, we report that Erv1 forms a 1:1 complex with cytochrome c and a reduced Erv1 can transfer electrons directly to the ferric form of the cytochrome. Erv1 also utilized molecular oxygen as an electron acceptor to generate hydrogen peroxide, which is subsequently reduced to water by cytochrome c peroxidase (Ccp1). Oxidized Ccp1 was in turn reduced by the Erv1-reduced cytochrome c. By coupling these pathways, cytochrome c and Ccp1 function efficiently as Erv1-dependent electron acceptors. Thus, we propose that Erv1 utilizes diverse pathways for electron shuttling in the IMS.
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“Erv1 serves to shuttle electrons from Mia40 to cytochrome c of the ETC in order to maintain its oxidized state (10, 40, 105, 292).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [105]
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Mesecke, N., Terziyska, N., Kozany, C., Baumann, F., Neupert, W., Hell, K., & Herrmann, J. M. (2005) · Cell · doi:10.1016/j.cell.2005.04.011 · Cited by 557
Protein Disulfide Bond Formation in Prokaryotes
Kadokura, H., Katzen, F., & Beckwith, J. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161459 · Cited by 554
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Chacińska, A., Pfannschmidt, S., Wiedemann, N., Kozjak‐Pavlovic, V., Szklarz, L. K. S., Schulze‐Specking, A., Truscott, K. N., Guiard, B., Meisinger, C., & Pfanner, N. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600389 · Cited by 464
Oxidative Protein Folding Is Driven by the Electron Transport System
Bader, M. W., Muse, W. B., Ballou, D. P., Gassner, C., & Bardwell, J. C. A. (1999) · Cell · doi:10.1016/s0092-8674(00)81016-8 · Cited by 385
Import of Mitochondrial Carriers Mediated by Essential Proteins of the Intermembrane Space
Koehler, C. M., Jarosch, E., Tokatlidis, K., Schmid, K., Schweyen, R. J., & Schatz, G. (1998) · Science · doi:10.1126/science.279.5349.369 · Cited by 326
Self-citationLange, H., Lisowsky, T., Gerber, J., Mühlenhoff, U., Kispál, G., & Lill, R. (2001) · EMBO Reports · doi:10.1093/embo-reports/kve161 · Cited by 269
Allen, S., Balabanidou, V., Sideris, D. P., Lisowsky, T., & Tokatlidis, K. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.08.049 · Cited by 235
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Herrmann, J. M., & Riemer, J. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3270 · Cited by 21
Kim, S. G., Chung, J.-S., Sutton, R. B., Lee, J.-S., López‐Maury, L., LEE, S., Florencio, F. J., Lin, T., Zabet‐Moghaddam, M., Wood, M. J., et al. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.10.012 · Cited by 20
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Specht, S., Liedgens, L., Duarte, M., Stiegler, A., Wirth, U., Eberhardt, M., Tomás, A. M., Hell, K., & Deponte, M. (2017) · Redox Biology · doi:10.1016/j.redox.2017.12.010 · Cited by 12
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Alder, N. N. (2011) · CRC Press eBooks · doi:10.1201/b11018-15 · Cited by 4
Cardenas‐Rodriguez, M., Manganas, P., Kallergi, E., Edwards, R., Chatzi, A., Lacko, E., & Tokatlidis, K. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.22.449413 · Cited by 4
Wang, Q., Ang, S. K., Ceh‐Pavia, E., Pang, J., & Lu, H. (2015) · Bioscience Reports · doi:10.1042/bsr20150144 · Cited by 3
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Marín-García, J. (2012) · Springer eBooks · doi:10.1007/978-1-4614-4599-9_4 · Cited by 1
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Becker, D., Seibold, U. K., & Voos, W. (2010) · Springer eBooks · doi:10.1007/978-0-387-89781-3_12
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Metadata
- Authors
- Dabir, D. V., Leverich, E. P., Kim, S., Tsai, F. D., Hirasawa, M., Knaff, D. B., & Koehler, C. M.
- Affiliations
- University of California, Los Angeles (US)
- Texas Tech University (US)
- Corresponding author
- Koehler, Carla M
- Venue
- The EMBO Journal
- Published
- 2007-11-01
- Volume
- 26
- Issue
- 23
- Pages
- 4801-4811
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC2099471
- OpenAlex
- W2020188627
- Cited by
- 162
- References
- 46
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 2 · 2023: 4 · 2022: 3 · 2021: 14 · 2020: 6 · 2019: 6 · 2018: 2 · 2017: 10 · 2016: 8 · 2015: 9 · 2014: 9 · 2013: 9 · 2012: 18
- FWCI
- 5.82
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Energy (FG0399ER20346)
- Welch Foundation
- American Heart Association (0640076N)
- Ohio State University
- Universität zu Köln
- National Institutes of Health
- U.S. Public Health Service
- National Institute of General Medical Sciences (F31GM070415, R01GM061721, GM070415)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- Erv1, cytochrome c, cytochrome c peroxidase, CCP1, electron shuttling, electron acceptors, mitochondrial intermembrane space, hydrogen peroxide, redox titration, electron transfer
- MeSH terms
- Alleles, Biochemistry, Cytochrome-c Peroxidase, Electrons, Hydrogen Peroxide, Models, Biological, Models, Genetic, Oxidation-Reduction, Oxygen, Saccharomyces cerevisiae, Time Factors, Protein Transport, Mitochondrial Proteins, Saccharomyces cerevisiae Proteins, Mitochondrial Membrane Transport Proteins, Cytochromes c, Oxidoreductases Acting on Sulfur Group Donors
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