Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Jonathan Lasham"'
Autor:
Liina Hannula, Suvi Kuivanen, Jonathan Lasham, Ravi Kant, Lauri Kareinen, Mariia Bogacheva, Tomas Strandin, Tarja Sironen, Jussi Hepojoki, Vivek Sharma, Petri Saviranta, Anja Kipar, Olli Vapalahti, Juha T. Huiskonen, Ilona Rissanen
Publikováno v:
Microbiology Spectrum, Vol 12, Iss 4 (2024)
ABSTRACTIn response to the ongoing COVID-19 pandemic, the quest for coronavirus inhibitors has inspired research on a variety of small proteins beyond conventional antibodies, including robust single-domain antibody fragments, i.e., “nanobodies.”
Externí odkaz:
https://doaj.org/article/cecbf8f257de4f2482e0413c26276bab
Respiratory complex I in mitochondria and bacteria catalyzes the transfer of electrons from NADH to quinone (Q). The free energy available from the reaction is used to pump protons and to establish a membrane proton electrochemical gradient, which dr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df193307cfc21239f5de6901e3c1f6ee
http://hdl.handle.net/10138/356023
http://hdl.handle.net/10138/356023
Publikováno v:
Chemical Science.
Respiratory complex I is a redox-driven proton pump contributing to about 40% of total proton motive force required for mitochondrial ATP generation. Recent high-resolution cryo-EM structural data revealed the positions of several water molecules in
Autor:
Tomoo Shiba, Takahiro Masuya, Daniel Ken Inaoka, Vivek Sharma, Masatoshi Murai, Outi Haapanen, Shinpei Uno, Kyoko Shinzawa-Itoh, Jonathan Lasham, Hideto Miyoshi
Publikováno v:
J Biol Chem
NADH-quinone oxidoreductase (complex I) couples electron transfer from NADH to quinone with proton translocation across the membrane. Quinone reduction is a key step for energy transmission from the site of quinone reduction to the remotely located p
Autor:
Liina Hannula, Suvi Kuivanen, Jonathan Lasham, Ravi Kant, Lauri Kareinen, Mariia Bogacheva, Tomas Strandin, Tarja Sironen, Vivek Sharma, Petri Saviranta, Anja Kipar, Olli Vapalahti, Juha T. Huiskonen, Ilona Rissanen
Publikováno v:
BioRxiv
bioRxiv
bioRxiv
In response to the ongoing SARS-CoV-2 pandemic, the quest for coronavirus inhibitors has inspired research on a variety of small proteins beyond conventional antibodies, including robust single-domain antibody fragments, ‘nanobodies’. Here, we ex
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:
Patryk Kuleta, Robert Ekiert, Jonathan Lasham, Arkadiusz Borek, Anna Wójcik-Augustyn, Vivek Sharma, Artur Osyczka
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1863:148745
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1863:148648
Autor:
Patryk Kuleta, Iwona Ekiert, Artur Osyczka, Marcin Sarewicz, Vivek Sharma, Jonathan Lasham, Robert Ekiert
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance To perform their specific electron-transfer relay functions, hemes commonly adopt low spin states with fine-tuned redox potentials. Understanding molecular elements controlling these properties is crucial for the description of natural p
Autor:
Shinpei Uno, Takahiro Masuya, Oleksii Zdorevskyi, Ryo Ikunishi, Kyoko Shinzawa-Itoh, Jonathan Lasham, Vivek Sharma, Masatoshi Murai, Hideto Miyoshi
Publikováno v:
Journal of Biological Chemistry. 298:102075
The ubiquinone (UQ) reduction step catalyzed by NADH-UQ oxidoreductase (mitochondrial respiratory complex I) is key to triggering proton translocation across the inner mitochondrial membrane. Structural studies have identified a long, narrow, UQ-acce