Kinetic coupling of the respiratory chain with ATP synthase, but not proton gradients, drives ATP production in cristae membranes.


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
04 02 2020
Historique:
pubmed: 23 1 2020
medline: 5 6 2020
entrez: 23 1 2020
Statut: ppublish

Résumé

Mitochondria have a characteristic ultrastructure with invaginations of the inner membrane called cristae that contain the protein complexes of the oxidative phosphorylation system. How this particular morphology of the respiratory membrane impacts energy conversion is currently unknown. One proposed role of cristae formation is to facilitate the establishment of local proton gradients to fuel ATP synthesis. Here, we determined the local pH values at defined sublocations within mitochondria of respiring yeast cells by fusing a pH-sensitive GFP to proteins residing in different mitochondrial subcompartments. Only a small proton gradient was detected over the inner membrane in wild type or cristae-lacking cells. Conversely, the obtained pH values did barely permit ATP synthesis in a reconstituted system containing purified yeast F

Identifiants

pubmed: 31964824
pii: 1917968117
doi: 10.1073/pnas.1917968117
pmc: PMC7007565
doi:

Substances chimiques

Proteolipids 0
Proton Pumps 0
Protons 0
proteoliposomes 0
Adenosine Triphosphate 8L70Q75FXE
Mitochondrial Proton-Translocating ATPases EC 3.6.3.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

2412-2421

Déclaration de conflit d'intérêts

The authors declare no competing interest.

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Auteurs

Alexandra Toth (A)

Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.

Axel Meyrat (A)

Department of Chemistry and Biochemistry, University of Bern, CH-3012 Bern, Switzerland.

Stefan Stoldt (S)

Department of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, DE-37077 Göttingen, Germany.

Ricardo Santiago (R)

Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.

Dirk Wenzel (D)

Laboratory of Electron Microscopy, Max Planck Institute for Biophysical Chemistry, DE-37077 Göttingen, Germany.

Stefan Jakobs (S)

Department of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, DE-37077 Göttingen, Germany.
Clinic of Neurology, University Medical Center Göttingen, DE-37075 Göttingen, Germany.

Christoph von Ballmoos (C)

Department of Chemistry and Biochemistry, University of Bern, CH-3012 Bern, Switzerland; christoph.vonballmoos@dcb.unibe.ch martin.ott@dbb.su.se.

Martin Ott (M)

Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden; christoph.vonballmoos@dcb.unibe.ch martin.ott@dbb.su.se.

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Classifications MeSH