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Sazanov Leonid A

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COST Action CA15203 (2016-2021): MitoEAGLE
Evolution-Age-Gender-Lifestyle-Environment: mitochondrial fitness mapping


Sazanov Leonid A


MitoPedia topics: EAGLE 

COST: Member COST WG1: WG1


Name Sazanov Leonid, Prof. FRS
Institution
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Institute of Science and Technology, IST Austria

Address Am Campus 1, A-3400
City Klosterneuburg
State/Province
Country Austria
Email [email protected]
Weblink
O2k-Network Lab

Bioenergetics Communications

Keywords: Complex I, ATP synthase, supercomplexes, proton translocation

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Publications

 PublishedReference
Sazanov 2023 Biochem J2023Sazanov LA (2023) From the 'black box' to 'domino effect' mechanism: what have we learned from the structures of respiratory complex I. Biochem J 480:319-33. https://doi.org/10.1042/BCJ20210285
Molina-Granada 2022 Commun Biol2022Molina-Granada D, González-Vioque E, Dibley MG, Cabrera-Pérez R, Vallbona-Garcia A, Torres-Torronteras J, Sazanov LA, Ryan MT, Cámara Y, Martí R (2022) Most mitochondrial dGTP is tightly bound to respiratory complex I through the NDUFA10 subunit. Commun Biol 5:620. doi: 10.1038/s42003-022-03568-6
Kravchuk 2022 Nature2022Kravchuk V, Petrova O, Kampjut D, Wojciechowska-Bason A, Breese Z, Sazanov L (2022) A universal coupling mechanism of respiratory complex I. Nature 609:808-14. https://doi.org/10.1038/s41586-022-05199-7. Erratum in: Nature. 2022;611:E9.
Kampjut 2022 Curr Opin Struct Biol2022Kampjut D, Sazanov LA (2022) Structure of respiratory complex I - An emerging blueprint for the mechanism. Curr Opin Struct Biol 74:102350. doi: 10.1016/j.sbi.2022.102350
Vercellino 2022 Nat Rev Mol Cell Biol2022Vercellino I, Sazanov LA (2022) The assembly, regulation and function of the mitochondrial respiratory chain. Nat Rev Mol Cell Biol 23:141-161. doi: 10.1038/s41580-021-00415-0
Vercellino 2021 Nature2021Vercellino I, Sazanov LA (2021) Structure and assembly of the mammalian mitochondrial supercomplex CIII2CIV. Nature 598:364-367. doi: 10.1038/s41586-021-03927-z
Kampjut 2020 Science2020Kampjut D, Sazanov LA (2020) The coupling mechanism of mammalian respiratory complex I. Science 370:eabc4209. https://doi.org/10.1126/science.abc4209
Pinke 2020 Nat Struct Mol Biol2020Pinke G, Zhou L, Sazanov LA (2020) Cryo-EM structure of the entire mammalian F-type ATP synthase. Nat Struct Mol Biol 27:1077-85. doi: 10.1038/s41594-020-0503-8
BEC 2020.1 doi10.26124bec2020-0001.v12020Gnaiger E et al ― MitoEAGLE Task Group (2020) Mitochondrial physiology. Bioenerg Commun 2020.1. https://doi.org/10.26124/bec:2020-0001.v1
Gutiérrez-Fernández 2020 Nat Commun2020Gutiérrez-Fernández J, Kaszuba K, Minhas GS, Baradaran R, Tambalo M, Gallagher DT, Sazanov LA (2020) Key role of quinone in the mechanism of respiratory complex I. Nat Commun 11:4135. doi: 10.1038/s41467-020-17957-0
Zhou 2019 Science2019Zhou L, Sazanov LA (2019) Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase. Science 365:eaaw9144. https://doi.org/10.1126/science.aaw9144
Letts 2019 Mol Cell2019Letts JA, Fiedorczuk K, Degliesposti G, Skehel M, Sazanov LA (2019) Structures of respiratory supercomplex I+III2 reveal functional and conformational crosstalk. Mol Cell 75:1131-46.e6. doi: 10.1016/j.molcel.2019.07.022
Kampjut 2019 Nature2019Kampjut D, Sazanov LA (2019) Structure and mechanism of mitochondrial proton-translocating transhydrogenase. Nature 573:291-5. doi: 10.1038/s41586-019-1519-2
Letts 2017 Nat Struct Mol Biol2017Letts JA, Sazanov LA (2017) Clarifying the supercomplex: the higher-order organization of the mitochondrial electron transport chain. Nat Struct Mol Biol 24:800-8. https://doi.org/10.1038/nsmb.3460
Letts 2016 Nature2016Letts JA, Fiedorczuk K, Sazanov LA (2016) The architecture of respiratory supercomplexes. Nature 537:644-8. https://doi.org/10.1038/nature19774
Sazanov 2015 Nat Rev Mol Cell Biol2015Sazanov LA (2015) A giant molecular proton pump: structure and mechanism of respiratory complex I. Nat Rev Mol Cell Biol 16:375-88. https://doi.org/10.1038/nrm3997
Letts 2015 Curr Opin Struct Biol2015Letts JA, Sazanov LA (2015) Gaining mass: the structure of respiratory complex I-from bacterial towards mitochondrial versions. Curr Opin Struct Biol 33:135-45. https://doi.org/10.1016/j.sbi.2015.08.008
Sazanov 2014 J Bioenerg Biomembr2014Sazanov LA (2014) The mechanism of coupling between electron transfer and proton translocation in respiratory complex I. J Bioenerg Biomembr 46:247-53. https://doi.org/10.1007/s10863-014-9554-z
Baradaran 2013 Nature2013Baradaran R, Berrisford JM, Minhas GS, Sazanov LA (2013) Crystal structure of the entire respiratory complex I. Nature 494:443-8. https://doi.org/10.1038/nature11871
Efremov 2011 Nature2011Efremov RG, Sazanov LA (2011) Structure of the membrane domain of respiratory complex I. Nature 476:414-20. https://doi.org/10.1038/nature10330
Efremov 2010 Nature2010Efremov RG, Baradaran R, Sazanov LA (2010) The architecture of respiratory complex I. Nature 465:441-5. https://doi.org/10.1038/nature09066
Hinchliffe 2005 Science2005Hinchliffe P, Sazanov LA (2005) Organization of iron-sulfur clusters in respiratory complex I. Science 309:771-4. https://doi.org/10.1126/science.1113988
Sazanov 2000 J Mol Biol2000Sazanov LA, Walker JE (2000) Cryo-electron crystallography of two sub-complexes of bovine complex I reveals the relationship between the membrane and peripheral arms. J Mol Biol 302:455-64. https://doi.org/10.1006/jmbi.2000.4079

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