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Träfflista för sökning "WFRF:(Scheller Henrik V.) srt2:(2005)"

Sökning: WFRF:(Scheller Henrik V.) > (2005)

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1.
  • Khrouchtchova, Anastassia, et al. (författare)
  • A previosly found thylakoid membrane protein of 14 kDa (TMP14) is a novel subunit of photosystem I and is designated PSI-P
  • 2005
  • Ingår i: FEBS Letters. - : Wiley. - 0014-5793. ; 579:21, s. 4808-4812
  • Tidskriftsartikel (refereegranskat)abstract
    • We show that the thylakoid membrane phosphoprotein TMP14 is a novel subunit of plant photosystem I (PSI). Blue native/SDS–PAGE and sucrose gradient fractionation demonstrated the association of the protein exclusively with PSI. We designate the protein PSI-P. The presence of PSI-P subunit in Arabidopsis mutants lacking other PSI subunits was analyzed and suggested a location in the proximity of PSI-L, -H and -O subunits. The PSI-P protein was not differentially phosphorylated in state 1 and state 2.
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2.
  • Klimmek, Frank, et al. (författare)
  • Structure of the higher plant light harvesting complex I : in vivo characterization and structural interdependence of the Lhca proteins.
  • 2005
  • Ingår i: Biochemistry. - 0006-2960. ; 44:8, s. 3065-73
  • Tidskriftsartikel (refereegranskat)abstract
    • We have investigated the structure of the higher plant light harvesting complex of photosystem I (LHCI) by analyzing PSI-LHCI particles isolated from a set of Arabidopsis plant lines, each lacking a specific Lhca (Lhca1-4) polypeptide. Functional antenna size measurements support the recent finding that there are four Lhca proteins per PSI in the crystal structure [Ben-Shem, A., Frolow, F., and Nelson, N. (2003) Nature 426, 630-635]. According to HPLC analyses the number of pigment molecules bound within the LHCI is higher than expected from reconstitution studies or analyses of isolated native LHCI. Comparison of the spectra of the particles from the different lines reveals chlorophyll absorption bands peaking at 696, 688, 665, and 655 nm that are not present in isolated PSI or LHCI. These bands presumably originate from "gap" or "linker" pigments that are cooperatively coordinated by the Lhca and/or PSI proteins, which we have tentatively localized in the PSI-LHCI complex.
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