Promotion of oxidative phosphorylation by complex I-anchored carbonic anhydrases?

Publikation: Beitrag in FachzeitschriftÜbersichtsarbeitForschungPeer-Review

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OriginalspracheEnglisch
Seiten (von - bis)64-71
Seitenumfang8
FachzeitschriftTrends in plant science
Jahrgang29
Ausgabenummer1
Frühes Online-Datum19 Jan. 2023
PublikationsstatusVeröffentlicht - Jan. 2024

Abstract

The mitochondrial NADH-dehydrogenase complex of the respiratory chain, known as complex I, includes a carbonic anhydrase (CA) module attached to its membrane arm on the matrix side in protozoans, algae, and plants. Its physiological role is so far unclear. Recent electron cryo-microscopy (cryo-EM) structures show that the CA module may directly provide protons for translocation across the inner mitochondrial membrane at complex I. CAs can have a central role in adjusting the proton concentration in the mitochondrial matrix. We suggest that CA anchoring in complex I represents the original configuration to secure oxidative phosphorylation (OXPHOS) in the context of early endosymbiosis. After development of ‘modern mitochondria’ with pronounced cristae structures, this anchoring became dispensable, but has been retained in protozoans, algae, and plants.

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Promotion of oxidative phosphorylation by complex I-anchored carbonic anhydrases? / Braun, Hans Peter; Klusch, Niklas.
in: Trends in plant science, Jahrgang 29, Nr. 1, 01.2024, S. 64-71.

Publikation: Beitrag in FachzeitschriftÜbersichtsarbeitForschungPeer-Review

Braun HP, Klusch N. Promotion of oxidative phosphorylation by complex I-anchored carbonic anhydrases? Trends in plant science. 2024 Jan;29(1):64-71. Epub 2023 Jan 19. doi: 10.1016/j.tplants.2023.07.007, 10.15488/15380
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abstract = "The mitochondrial NADH-dehydrogenase complex of the respiratory chain, known as complex I, includes a carbonic anhydrase (CA) module attached to its membrane arm on the matrix side in protozoans, algae, and plants. Its physiological role is so far unclear. Recent electron cryo-microscopy (cryo-EM) structures show that the CA module may directly provide protons for translocation across the inner mitochondrial membrane at complex I. CAs can have a central role in adjusting the proton concentration in the mitochondrial matrix. We suggest that CA anchoring in complex I represents the original configuration to secure oxidative phosphorylation (OXPHOS) in the context of early endosymbiosis. After development of {\textquoteleft}modern mitochondria{\textquoteright} with pronounced cristae structures, this anchoring became dispensable, but has been retained in protozoans, algae, and plants.",
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author = "Braun, {Hans Peter} and Niklas Klusch",
note = "Funding Information: We thank Werner K{\"u}hlbrandt and Jennifer Senkler for critically reading the manuscript. The research in our laboratories is funded by the Max Planck Society (N.K.) and the Deutsche Forschungsgemeinschaft (grant INST 187/791-1 FUGG to H-P.B.). ",
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AU - Braun, Hans Peter

AU - Klusch, Niklas

N1 - Funding Information: We thank Werner Kühlbrandt and Jennifer Senkler for critically reading the manuscript. The research in our laboratories is funded by the Max Planck Society (N.K.) and the Deutsche Forschungsgemeinschaft (grant INST 187/791-1 FUGG to H-P.B.).

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N2 - The mitochondrial NADH-dehydrogenase complex of the respiratory chain, known as complex I, includes a carbonic anhydrase (CA) module attached to its membrane arm on the matrix side in protozoans, algae, and plants. Its physiological role is so far unclear. Recent electron cryo-microscopy (cryo-EM) structures show that the CA module may directly provide protons for translocation across the inner mitochondrial membrane at complex I. CAs can have a central role in adjusting the proton concentration in the mitochondrial matrix. We suggest that CA anchoring in complex I represents the original configuration to secure oxidative phosphorylation (OXPHOS) in the context of early endosymbiosis. After development of ‘modern mitochondria’ with pronounced cristae structures, this anchoring became dispensable, but has been retained in protozoans, algae, and plants.

AB - The mitochondrial NADH-dehydrogenase complex of the respiratory chain, known as complex I, includes a carbonic anhydrase (CA) module attached to its membrane arm on the matrix side in protozoans, algae, and plants. Its physiological role is so far unclear. Recent electron cryo-microscopy (cryo-EM) structures show that the CA module may directly provide protons for translocation across the inner mitochondrial membrane at complex I. CAs can have a central role in adjusting the proton concentration in the mitochondrial matrix. We suggest that CA anchoring in complex I represents the original configuration to secure oxidative phosphorylation (OXPHOS) in the context of early endosymbiosis. After development of ‘modern mitochondria’ with pronounced cristae structures, this anchoring became dispensable, but has been retained in protozoans, algae, and plants.

KW - carbonic anhydrase

KW - endosymbiotic theory

KW - mitochondria

KW - mitochondrial evolution

KW - NADH dehydrogenase complex (complex I)

KW - Oxidative Phosphorylation (OXPHOS)

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U2 - 10.1016/j.tplants.2023.07.007

DO - 10.1016/j.tplants.2023.07.007

M3 - Review article

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VL - 29

SP - 64

EP - 71

JO - Trends in plant science

JF - Trends in plant science

SN - 1360-1385

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ER -

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