dc.contributor.author
Ataka, Kenichi
dc.contributor.author
Stripp, Sven
dc.contributor.author
Heberle, Joachim
dc.date.accessioned
2018-06-08T04:00:18Z
dc.date.available
2014-09-09T18:53:24.617Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/16388
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-20570
dc.description.abstract
Surface-enhanced infrared absorption spectroscopy (SEIRAS) represents a
variation of conventional infrared spectroscopy and exploits the signal
enhancement exerted by the plasmon resonance of nano-structured metal thin
films. The surface enhancement decays in about 10 nm with the distance from
the surface and is, thus, perfectly suited to selectively probe monolayers of
biomembranes. Peculiar to membrane proteins is their vectorial functionality,
the probing of which requires proper orientation within the membrane. To this
end, the metal surface used in SEIRAS is chemically modified to generate an
oriented membrane protein film. Monolayers of uniformly oriented membrane
proteins are formed by tethering His-tagged proteins to a nickel nitrilo-
triacetic acid (Ni-NTA) modified gold surface and SEIRAS commands molecular
sensitivity to probe each step of surface modification. The solid surface used
as plasmonic substrate for SEIRAS, can also be employed as an electrode to
investigate systems where electron transfer reactions are relevant, like e.g.
cytochrome c oxidase or plant-type photosystems. Furthermore, the interaction
of these membrane proteins with water-soluble proteins, like cytochrome c or
hydrogenase, is studied on the molecular level by SEIRAS. The impact of the
membrane potential on protein functionality is verified by monitoring
light–dark difference spectra of a monolayer of sensory rhodopsin (SRII) at
different applied potentials. It is demonstrated that the interpretations of
all of these experiments critically depend on the orientation of the solid-
supported membrane protein. Finally, future directions of SEIRAS including
cellular systems are discussed. This article is part of a Special Issue
entitled: FTIR in membrane proteins and peptide studies.
en
dc.rights.uri
http://www.elsevier.com/about/open-access/green-open-access
dc.subject
Proton transfer
dc.subject
Cytochrome c oxidase
dc.subject.ddc
500 Naturwissenschaften und Mathematik::530 Physik
dc.title
Surface-enhanced infrared absorption spectroscopy (SEIRAS) to probe monolayers
of membrane proteins
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation
Biochimica et Biophysica Acta (BBA) - Biomembranes. - 1828 (2013), 10, S.
2283-2293
dc.identifier.sepid
31799
dcterms.bibliographicCitation.doi
10.1016/j.bbamem.2013.04.026
dcterms.bibliographicCitation.url
http://dx.doi.org/10.1016/j.bbamem.2013.04.026
refubium.affiliation
Physik
de
refubium.affiliation.other
Institut für Experimentalphysik
refubium.mycore.fudocsId
FUDOCS_document_000000020926
refubium.resourceType.isindependentpub
no
refubium.mycore.derivateId
FUDOCS_derivate_000000003882
dcterms.accessRights.openaire
open access
dcterms.isPartOf.issn
00052736