Redox- and protonation-state driven substrate-protein dynamics in respiratory complex I

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http://hdl.handle.net/10138/335511

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Haapanen , O & Sharma , V 2021 , ' Redox- and protonation-state driven substrate-protein dynamics in respiratory complex I ' , Current opinion in electrochemistry , vol. 29 , 100741 . https://doi.org/10.1016/j.coelec.2021.100741

Titel: Redox- and protonation-state driven substrate-protein dynamics in respiratory complex I
Författare: Haapanen, Outi; Sharma, Vivek
Upphovmannens organisation: Materials Physics
Department of Physics
Institute of Biotechnology
Datum: 2021-10
Språk: eng
Sidantal: 6
Tillhör serie: Current opinion in electrochemistry
ISSN: 2451-9103
DOI: https://doi.org/10.1016/j.coelec.2021.100741
Permanenta länken (URI): http://hdl.handle.net/10138/335511
Abstrakt: Respiratory complex I is a key enzyme in the electron transport chains of mitochondria and bacteria. It transfers two electrons to quinone and couples this redox reaction to proton pumping to electrically charge the membrane it is embedded in. The charge and pH gradient across the membrane drives the synthesis of ATP. The redox reaction and proton pumping in complex I are separated in space and time, which raises the question of how the two reactions are coupled so efficiently. Here, we focus on the unique similar to 35 angstrom long tunnel of complex I, which houses the binding site of quinone reduction. We discuss the redox and protonation reactions that occur in this tunnel and how they influence the dynamics of protein and substrate. On the basis of recent structural data and results from molecular simulations, we review how quinone reduction and dynamics may be coupled to proton pumping in complex I.
Subject: Electron transfer
Proton pumping
Quantum chemistry
Molecular dynamics simulations
UBIQUINONE BINDING
CRYSTAL-STRUCTURE
BOUND UBIQUINONE
CLUSTER N2
MECHANISM
SUBUNIT
MEMBRANE
RESIDUES
TYROSINE
SITE
114 Physical sciences
Referentgranskad: Ja
Licens: cc_by
Användningsbegränsning: openAccess
Parallelpublicerad version: publishedVersion


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