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Structural characterization of a plant photosystem I and NAD(P)H dehydrogenase supercomplex
R. Kouřil, O. Strouhal, L. Nosek, R. Lenobel, I. Chamrád, EJ. Boekema, M. Šebela, P. Ilík,
Jazyk angličtina Země Anglie, Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Free Medical Journals
od 1991 do Před 1 rokem
Wiley Free Content
od 1997 do Před 1 rokem
PubMed
24313886
DOI
10.1111/tpj.12402
Knihovny.cz E-zdroje
- MeSH
- elektronová mikroskopie MeSH
- ferredoxiny metabolismus MeSH
- fotosystém I - proteinový komplex chemie izolace a purifikace metabolismus MeSH
- ječmen (rod) chemie enzymologie účinky záření MeSH
- listy rostlin chemie enzymologie účinky záření MeSH
- molekulární modely MeSH
- NAD metabolismus MeSH
- NADPH-dehydrogenasa chemie izolace a purifikace metabolismus MeSH
- nativní elektroforéza na polyakrylamidovém gelu MeSH
- oxidace-redukce MeSH
- světlo MeSH
- světlosběrné proteinové komplexy chemie izolace a purifikace metabolismus MeSH
- transport elektronů MeSH
- tylakoidy metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
Cyclic electron transport (CET) around photosystem I (PSI) plays an important role in balancing the ATP/NADPH ratio and the photoprotection of plants. The NAD(P)H dehydrogenase complex (NDH) has a key function in one of the CET pathways. Current knowledge indicates that, in order to fulfill its role in CET, the NDH complex needs to be associated with PSI; however, until now there has been no direct structural information about such a supercomplex. Here we present structural data obtained for a plant PSI-NDH supercomplex. Electron microscopy analysis revealed that in this supercomplex two copies of PSI are attached to one NDH complex. A constructed pseudo-atomic model indicates asymmetric binding of two PSI complexes to NDH and suggests that the low-abundant Lhca5 and Lhca6 subunits mediate the binding of one of the PSI complexes to NDH. On the basis of our structural data, we propose a model of electron transport in the PSI-NDH supercomplex in which the association of PSI to NDH seems to be important for efficient trapping of reduced ferredoxin by NDH.
Citace poskytuje Crossref.org
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