Effects of Liposome and Cardiolipin on Folding and Function of Mitochondrial Erv1
Erv1 (EC number 1.8.3.2) is an essential mitochondrial enzyme catalyzing protein import and oxidative folding in the mitochondrial intermembrane space. Erv1 has both oxidase and cytochrome <i>c</i> reductase activities. While both Erv1 and cytochrome <i>c</i> were reported to...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-12-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/21/24/9402 |
| _version_ | 1797545134404927488 |
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| author | Xiaofan Tang Lynda K Harris Hui Lu |
| author_facet | Xiaofan Tang Lynda K Harris Hui Lu |
| author_sort | Xiaofan Tang |
| collection | DOAJ |
| description | Erv1 (EC number 1.8.3.2) is an essential mitochondrial enzyme catalyzing protein import and oxidative folding in the mitochondrial intermembrane space. Erv1 has both oxidase and cytochrome <i>c</i> reductase activities. While both Erv1 and cytochrome <i>c</i> were reported to be membrane associated in mitochondria, it is unknown how the mitochondrial membrane environment may affect the function of Erv1. Here, in this study, we used liposomes to mimic the mitochondrial membrane and investigated the effect of liposomes and cardiolipin on the folding and function of yeast Erv1. Enzyme kinetics of both the oxidase and cytochrome <i>c</i> reductase activity of Erv1 were studied using oxygen consumption analysis and spectroscopic methods. Our results showed that the presence of liposomes has mild impacts on Erv1 oxidase activity, but significantly inhibited the catalytic efficiency of Erv1 cytochrome <i>c</i> reductase activity in a cardiolipin-dependent manner. Taken together, the results of this study provide important insights into the function of Erv1 in the mitochondria, suggesting that molecular oxygen is a better substrate than cytochrome <i>c</i> for Erv1 in the yeast mitochondria. |
| first_indexed | 2024-03-10T14:11:09Z |
| format | Article |
| id | doaj.art-d0535bbf43d940598197c6418a097b04 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T14:11:09Z |
| publishDate | 2020-12-01 |
| publisher | MDPI AG |
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| series | International Journal of Molecular Sciences |
| spelling | doaj.art-d0535bbf43d940598197c6418a097b042023-11-21T00:15:09ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-12-012124940210.3390/ijms21249402Effects of Liposome and Cardiolipin on Folding and Function of Mitochondrial Erv1Xiaofan Tang0Lynda K Harris1Hui Lu2School of Biological Sciences, Faculty of Biology, Medicine and Health, The University of Manchester, Manchester M13 9PT, UKDivision of Pharmacy and Optometry, School of Health Sciences, Faculty of Biology, Medicine and Health, The University of Manchester, Manchester M13 9PL, UKSchool of Biological Sciences, Faculty of Biology, Medicine and Health, The University of Manchester, Manchester M13 9PT, UKErv1 (EC number 1.8.3.2) is an essential mitochondrial enzyme catalyzing protein import and oxidative folding in the mitochondrial intermembrane space. Erv1 has both oxidase and cytochrome <i>c</i> reductase activities. While both Erv1 and cytochrome <i>c</i> were reported to be membrane associated in mitochondria, it is unknown how the mitochondrial membrane environment may affect the function of Erv1. Here, in this study, we used liposomes to mimic the mitochondrial membrane and investigated the effect of liposomes and cardiolipin on the folding and function of yeast Erv1. Enzyme kinetics of both the oxidase and cytochrome <i>c</i> reductase activity of Erv1 were studied using oxygen consumption analysis and spectroscopic methods. Our results showed that the presence of liposomes has mild impacts on Erv1 oxidase activity, but significantly inhibited the catalytic efficiency of Erv1 cytochrome <i>c</i> reductase activity in a cardiolipin-dependent manner. Taken together, the results of this study provide important insights into the function of Erv1 in the mitochondria, suggesting that molecular oxygen is a better substrate than cytochrome <i>c</i> for Erv1 in the yeast mitochondria.https://www.mdpi.com/1422-0067/21/24/9402sulfhydryl oxidaseMIA pathwaymitochondrial membraneenzyme kinetics |
| spellingShingle | Xiaofan Tang Lynda K Harris Hui Lu Effects of Liposome and Cardiolipin on Folding and Function of Mitochondrial Erv1 International Journal of Molecular Sciences sulfhydryl oxidase MIA pathway mitochondrial membrane enzyme kinetics |
| title | Effects of Liposome and Cardiolipin on Folding and Function of Mitochondrial Erv1 |
| title_full | Effects of Liposome and Cardiolipin on Folding and Function of Mitochondrial Erv1 |
| title_fullStr | Effects of Liposome and Cardiolipin on Folding and Function of Mitochondrial Erv1 |
| title_full_unstemmed | Effects of Liposome and Cardiolipin on Folding and Function of Mitochondrial Erv1 |
| title_short | Effects of Liposome and Cardiolipin on Folding and Function of Mitochondrial Erv1 |
| title_sort | effects of liposome and cardiolipin on folding and function of mitochondrial erv1 |
| topic | sulfhydryl oxidase MIA pathway mitochondrial membrane enzyme kinetics |
| url | https://www.mdpi.com/1422-0067/21/24/9402 |
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