Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Etienne Galemou Yoga"'
Autor:
Etienne Galemou Yoga, Kristian Parey, Amina Djurabekova, Outi Haapanen, Karin Siegmund, Klaus Zwicker, Vivek Sharma, Volker Zickermann, Heike Angerer
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-8 (2020)
Respiratory complex I plays a key role in energy metabolism. Cryo-EM structure of a mutant accessory subunit LYRM6 from the yeast Yarrowia lipolytica and molecular dynamics simulations reveal conformational changes at the interface between LYRM6 and
Externí odkaz:
https://doaj.org/article/89bb52ee11ed43a19deeb0190964dfe0
Publikováno v:
Frontiers in Chemistry, Vol 9 (2021)
NADH: ubiquinone oxidoreductase (complex I) is the first enzyme complex of the respiratory chain. Complex I is a redox-driven proton pump that contributes to the proton motive force that drives ATP synthase. The structure of complex I has been analyz
Externí odkaz:
https://doaj.org/article/16481c55996046708eb82ffecfcd7793
Autor:
Alfredo Cabrera-Orefice, Etienne Galemou Yoga, Christophe Wirth, Karin Siegmund, Klaus Zwicker, Sergio Guerrero-Castillo, Volker Zickermann, Carola Hunte, Ulrich Brandt
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
Proton pumping of mitochondrial complex I depends on the reduction of ubiquinone but the molecular mechanism of energy conversion is unclear. Here, the authors provide structural and biochemical evidence showing that movement of loop TMH1-2 in comple
Externí odkaz:
https://doaj.org/article/6efa54739f774befb5b738b28df7f4b2
Autor:
Amina Djurabekova, Etienne Galemou Yoga, Aino Nyman, Antti Pirttikoski, Volker Zickermann, Outi Haapanen, Vivek Sharma
Publikováno v:
FEBS lettersReferences. 596(9)
The first component of the mitochondrial electron transport chain is respiratory complex I. Several high-resolution structures of complex I from different species have been resolved. However, despite these significant achievements, the mechanism of r
Autor:
Volker Zickermann, Janet Vonck, Jonathan Lasham, Vivek Sharma, Hao Xie, Deryck J. Mills, Etienne Galemou Yoga, Amina Djurabekova, Kristian Parey, Outi Haapanen, Werner Kühlbrandt
Publikováno v:
Science Advances
Description
High-resolution structure and molecular simulations unravel the inner workings of a redox-driven proton pump.
Mitochondrial NADH:ubiquinone oxidoreductase (complex I) is a 1-MDa membrane protein complex with a central role in en
High-resolution structure and molecular simulations unravel the inner workings of a redox-driven proton pump.
Mitochondrial NADH:ubiquinone oxidoreductase (complex I) is a 1-MDa membrane protein complex with a central role in en
Autor:
Werner Kühlbrandt, Vivek Sharma, Amina Djurabekova, Hao Xie, Kristian Parey, Outi Haapanen, Janet Vonck, Etienne Galemou Yoga, Jonathan Lasham, Deryck J. Mills, Volker Zickermann
SummaryMitochondrial NADH:ubiquinone oxidoreductase (complex I) is a 1 MDa membrane protein complex with a central role in energy metabolism. Redox-driven proton translocation by complex I contributes substantially to the proton motive force that dri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b2627c01b769950d6896d83c45faa2e5
https://doi.org/10.1101/2021.04.16.440187
https://doi.org/10.1101/2021.04.16.440187
Autor:
Sergio Guerrero-Castillo, Klaus Zwicker, Etienne Galemou Yoga, Ulrich Brandt, Christophe Wirth, Carola Hunte, Alfredo Cabrera-Orefice, Karin Siegmund, Volker Zickermann
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
Nature Communications, 9
Nature Communications
Nature Communications, 9
Nature Communications
Complex I (proton-pumping NADH:ubiquinone oxidoreductase) is the largest enzyme of the mitochondrial respiratory chain and a significant source of reactive oxygen species (ROS). We hypothesized that during energy conversion by complex I, electron tra
Autor:
Swathi Banthiya, Mats Hamberg, Jacqueline Kalms, Patrick Scheerer, Xavi Carpena, Hartmut Kühn, Igor Ivanov, Etienne Galemou Yoga
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
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Pseudomonas aeruginosa expresses a secreted LOX-isoform (PA-LOX, LoxA) capable of oxidizing polyenoic fatty acids to hydroperoxy derivatives. Here we report high-level expression of this enzyme in E. coli and its structural and functional characteriz
Autor:
Outi Haapanen, Vivek Sharma, Volker Zickermann, Ilka Wittig, Etienne Galemou Yoga, Karin Siegmund
Respiratory complex I catalyses the reduction of ubiquinone (Q) from NADH coupled to proton pumping across the inner membrane of mitochondria. The electrical charging of the inner mitochondrial membrane drives the synthesis of ATP, which is used to p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6772f594fd8c9f80e70becc80f5ddc54
http://hdl.handle.net/10138/304764
http://hdl.handle.net/10138/304764
Autor:
Swathi Banthiya, Mats Hamberg, Hermann-Georg Holzhütter, Etienne Galemou Yoga, Hartmut Kühn, Patrick Scheerer, Jacqueline Kalms
Publikováno v:
Biochimica et biophysica acta. Molecular and cell biology of lipids. 1862(5)
Secreted LOX from Pseudomonas aeruginosa (PA-LOX) has previously been identified as arachidonic acid 15S-lipoxygenating enzyme. Here we report that the substitution of Ala420Gly in PA-LOX leads to an enzyme variant with pronounced dual specificity fa