<div class="csl-bib-body">
<div class="csl-entry">Srajer, J., Schwaighofer, A., Hildenbrandt, D. M., Kibrom, A., & Naumann, R. L. C. (2013). A kinetic model of proton transport in a multi-redox centre protein: cytochrome coxidase. <i>Progress in Reaction Kinetics and Mechanism</i>. https://doi.org/10.3184/146867812X13558465325118</div>
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The final publication is available via <a href="https://doi.org/10.3184/146867812X13558465325118" target="_blank">https://doi.org/10.3184/146867812X13558465325118</a>
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dc.description.abstract
We use chemical reaction kinetics to explore the stepwise electron and proton transfer reactions of cytochrome c oxidase (CcO) from R. sphaeroides. Proton transport coupled to electron transport (ET) is investigated in terms of a sequence of protonation-dependent second-order redox reactions. Thereby, we assume fixed rather than shifting dissociation constants of the redox sites. Proton transport can thus be simulated particularly when separate proton uptake and release sites are assumed rather than the same proton pump site for every ET step. In order to test these assumptions, we make use of a model system introduced earlier, which allows us to study direct ET of redox enzymes by electrochemistry. A four-electron transfer model of CcO had been developed before, according to which electrons are transferred from the electrode to CuA. Thereafter, electrons are transferred along the sequence heme a, heme a3 and CuB. In the present investigation, we consider protonation equilibria of the oxidised and reduced species for each of the four centres. Moreover, we add oxygen/H2O as the terminal (fifth) redox couple including protonation of reduced oxygen to water. Finally we arrive at a kinetic model comprising five protonation-dependent redox couples. The results from the simulations are compared with experimental data obtained in the absence and presence of oxygen. As a result, we can show that proton transport can be modelled in terms of protonation-dependent redox kinetics.
en
dc.language
English
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dc.language.iso
en
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dc.publisher
Sage Publications
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dc.relation.ispartof
Progress in Reaction Kinetics and Mechanism
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dc.rights.uri
http://rightsstatements.org/vocab/InC/1.0/
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dc.subject
proton pump
en
dc.subject
protonation-dependent chemical reaction kinetics
en
dc.subject
second-order redox reaction
en
dc.subject
metalloprotein
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dc.subject
master equation
en
dc.title
A kinetic model of proton transport in a multi-redox centre protein: cytochrome coxidase
en
dc.type
Article
en
dc.type
Artikel
de
dc.rights.license
Urheberrechtsschutz
de
dc.rights.license
In Copyright
en
dc.contributor.affiliation
Austrian Institute of Technology GmbH, Österreich
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dc.contributor.affiliation
Austrian Institute of Technology, Österreich
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dc.contributor.affiliation
Austrian Institute of Technology GmbH, Österreich
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dc.contributor.affiliation
Austrian Institute of Technology GmbH, Österreich
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dc.rights.holder
2013 by SAGE Publications
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dc.type.category
Original Research Article
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tuw.journal.peerreviewed
true
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tuw.peerreviewed
true
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tuw.version
am
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dcterms.isPartOf.title
Progress in Reaction Kinetics and Mechanism
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tuw.publication.orgunit
E164 - Institut für Chemische Technologien und Analytik
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tuw.publisher.doi
10.3184/146867812X13558465325118
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dc.identifier.eissn
1471-406X
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dc.identifier.libraryid
AC15520863
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dc.identifier.urn
urn:nbn:at:at-ubtuw:3-7625
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tuw.author.orcid
0000-0003-2714-7056
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dc.rights.identifier
Urheberrechtsschutz
de
dc.rights.identifier
In Copyright
en
wb.sci
true
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item.languageiso639-1
en
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item.fulltext
with Fulltext
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item.openaccessfulltext
Open Access
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application/pdf
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research article
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item.grantfulltext
open
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http://purl.org/coar/resource_type/c_2df8fbb1
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item.cerifentitytype
Publications
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crisitem.author.dept
TU Wien
-
crisitem.author.dept
E164-02-1 - Forschungsgruppe Prozessanalytik
-
crisitem.author.dept
Austrian Institute of Technology, Österreich
-
crisitem.author.dept
Austrian Institute of Technology GmbH, Österreich
-
crisitem.author.orcid
0000-0003-2714-7056
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crisitem.author.parentorg
E164-02 - Forschungsbereich Umwelt-, Prozessanalytik und Sensoren