Details
Originalsprache | Englisch |
---|---|
Seiten (von - bis) | 64-71 |
Seitenumfang | 8 |
Fachzeitschrift | Trends in plant science |
Jahrgang | 29 |
Ausgabenummer | 1 |
Frühes Online-Datum | 19 Jan. 2023 |
Publikationsstatus | Veröffentlicht - 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.
ASJC Scopus Sachgebiete
- Agrar- und Biowissenschaften (insg.)
- Pflanzenkunde
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in: Trends in plant science, Jahrgang 29, Nr. 1, 01.2024, S. 64-71.
Publikation: Beitrag in Fachzeitschrift › Übersichtsarbeit › Forschung › Peer-Review
}
TY - JOUR
T1 - Promotion of oxidative phosphorylation by complex I-anchored carbonic anhydrases?
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.).
PY - 2024/1
Y1 - 2024/1
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)
UR - http://www.scopus.com/inward/record.url?scp=85168382724&partnerID=8YFLogxK
U2 - 10.1016/j.tplants.2023.07.007
DO - 10.1016/j.tplants.2023.07.007
M3 - Review article
AN - SCOPUS:85168382724
VL - 29
SP - 64
EP - 71
JO - Trends in plant science
JF - Trends in plant science
SN - 1360-1385
IS - 1
ER -