Cited by 162Mitochondrial Function and PathologyRedox biology and oxidative stressEnzyme Structure and Function

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A role for cytochrome c and cytochrome c peroxidase in electron shuttling from Erv1

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Dabir, Deepa V, Leverich, Edward P, Kim, Sung‐Kun, Tsai, Frederick D, Hirasawa, Masakazu, Knaff, David B, Koehler, Carla M·2007·The EMBO Journal

DOI 10.1038/sj.emboj.7601909PMC PMC2099471

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Abstract

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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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
ORCID: Dabir, Deepa V
Kim, Sung‐Kun
Tsai, Frederick D
Koehler, Carla M
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 2007-11-01
Volume: 26
Issue: 23
Pages: 4801-4811
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1038/sj.emboj.7601909
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: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
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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A role for cytochrome c and cytochrome c peroxidase in electron shuttling from Erv1

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