dc.contributor.author
Lokstein, Heiko
dc.contributor.author
Renger, Gernot
dc.contributor.author
Götze, Jan P.
dc.date.accessioned
2021-06-28T13:37:36Z
dc.date.available
2021-06-28T13:37:36Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/31205
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-30941
dc.description.abstract
Chlorophylls and bacteriochlorophylls, together with carotenoids, serve, noncovalently bound to specific apoproteins, as principal light-harvesting and energy-transforming pigments in photosynthetic organisms. In recent years, enormous progress has been achieved in the elucidation of structures and functions of light-harvesting (antenna) complexes, photosynthetic reaction centers and even entire photosystems. It is becoming increasingly clear that light-harvesting complexes not only serve to enlarge the absorption cross sections of the respective reaction centers but are vitally important in short- and long-term adaptation of the photosynthetic apparatus and regulation of the energy-transforming processes in response to external and internal conditions. Thus, the wide variety of structural diversity in photosynthetic antenna “designs” becomes conceivable. It is, however, common for LHCs to form trimeric (or multiples thereof) structures. We propose a simple, tentative explanation of the trimer issue, based on the 2D world created by photosynthetic membrane systems.
en
dc.format.extent
24 Seiten
dc.rights.uri
https://creativecommons.org/licenses/by/4.0/
dc.subject
bacteriochlorophylls
en
dc.subject
chlorophylls
en
dc.subject
excitation energy transfer
en
dc.subject
light-harvesting complexes
en
dc.subject
photosynthesis
en
dc.subject
pigment-protein complexes
en
dc.subject
photosystems
en
dc.subject.ddc
500 Naturwissenschaften und Mathematik::540 Chemie::540 Chemie und zugeordnete Wissenschaften
dc.subject.ddc
500 Naturwissenschaften und Mathematik::540 Chemie::541 Physikalische Chemie
dc.title
Photosynthetic Light-Harvesting (Antenna) Complexes - Structures and Functions
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation.articlenumber
3378
dcterms.bibliographicCitation.doi
10.3390/molecules26113378
dcterms.bibliographicCitation.journaltitle
Molecules
dcterms.bibliographicCitation.number
11
dcterms.bibliographicCitation.originalpublishername
MDPI
dcterms.bibliographicCitation.volume
26
dcterms.bibliographicCitation.url
https://doi.org/10.3390/molecules26113378
refubium.affiliation
Biologie, Chemie, Pharmazie
refubium.affiliation.other
Institut für Chemie und Biochemie / Computational Chemistry and Theoretical Biophysics
refubium.resourceType.isindependentpub
no
dcterms.accessRights.openaire
open access
dcterms.isPartOf.eissn
1420-3049