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

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dc.contributor.author Haapanen, Outi
dc.contributor.author Sharma, Vivek
dc.date.accessioned 2021-10-21T05:21:02Z
dc.date.available 2021-10-21T05:21:02Z
dc.date.issued 2021-10
dc.identifier.citation 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
dc.identifier.other PURE: 169656376
dc.identifier.other PURE UUID: eea1ab8a-b4e1-4e06-b8c2-0da25a926d0b
dc.identifier.other WOS: 000704374600031
dc.identifier.other ORCID: /0000-0002-8838-3151/work/101864872
dc.identifier.uri http://hdl.handle.net/10138/335511
dc.description.abstract 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. en
dc.format.extent 6
dc.language.iso eng
dc.relation.ispartof Current opinion in electrochemistry
dc.rights cc_by
dc.rights.uri info:eu-repo/semantics/openAccess
dc.subject Electron transfer
dc.subject Proton pumping
dc.subject Quantum chemistry
dc.subject Molecular dynamics simulations
dc.subject UBIQUINONE BINDING
dc.subject CRYSTAL-STRUCTURE
dc.subject BOUND UBIQUINONE
dc.subject CLUSTER N2
dc.subject MECHANISM
dc.subject SUBUNIT
dc.subject MEMBRANE
dc.subject RESIDUES
dc.subject TYROSINE
dc.subject SITE
dc.subject 114 Physical sciences
dc.title Redox- and protonation-state driven substrate-protein dynamics in respiratory complex I en
dc.type Review Article
dc.contributor.organization Materials Physics
dc.contributor.organization Department of Physics
dc.contributor.organization Institute of Biotechnology
dc.description.reviewstatus Peer reviewed
dc.relation.doi https://doi.org/10.1016/j.coelec.2021.100741
dc.relation.issn 2451-9103
dc.rights.accesslevel openAccess
dc.type.version publishedVersion

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