dc.contributor.author
Zhang, Miao
dc.contributor.author
Bommer, Martin
dc.contributor.author
Chatterjee, Ruchira
dc.contributor.author
Hussein, Rana
dc.contributor.author
Yano, Junko
dc.contributor.author
Dau, Holger
dc.contributor.author
Kern, Jan
dc.contributor.author
Dobbek, Holger
dc.contributor.author
Zouni, Athina
dc.date.accessioned
2018-06-08T11:05:01Z
dc.date.available
2017-09-08T08:40:30.958Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/21592
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-24882
dc.description.abstract
In plants, algae and cyanobacteria, Photosystem II (PSII) catalyzes the light-
driven splitting of water at a protein-bound Mn4CaO5-cluster, the water-
oxidizing complex (WOC). In the photosynthetic organisms, the light-driven
formation of the WOC from dissolved metal ions is a key process because it is
essential in both initial activation and continuous repair of PSII. Structural
information is required for understanding of this chaperone-free metal-cluster
assembly. For the first time, we obtained a structure of PSII from
Thermosynechococcus elongatus without the Mn4CaO5-cluster. Surprisingly,
cluster-removal leaves the positions of all coordinating amino acid residues
and most nearby water molecules largely unaffected, resulting in a pre-
organized ligand shell for kinetically competent and error-free photo-assembly
of the Mn4CaO5-cluster. First experiments initiating (i) partial disassembly
and (ii) partial re-assembly after complete depletion of the Mn4CaO5-cluster
agree with a specific bi-manganese cluster, likely a di-µ-oxo bridged pair of
Mn(III) ions, as an assembly intermediate.
en
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.subject.ddc
500 Naturwissenschaften und Mathematik::500 Naturwissenschaften
dc.title
Structural insights into the light-driven auto-assembly process of the water-
oxidizing Mn4CaO5-cluster in photosystem II
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation
eLife. - 6 (2017), Artikel Nr. e26933
dcterms.bibliographicCitation.doi
10.7554/eLife.26933
dcterms.bibliographicCitation.url
http://doi.org/10.7554/eLife.26933.001
refubium.affiliation
Biologie, Chemie, Pharmazie
de
refubium.mycore.fudocsId
FUDOCS_document_000000027890
refubium.note.author
Der Artikel wurde in einer reinen Open-Access-Zeitschrift publiziert.
refubium.resourceType.isindependentpub
no
refubium.mycore.derivateId
FUDOCS_derivate_000000008714
dcterms.accessRights.openaire
open access