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Journal Article
Characterization of the Porphyridium cruentum Chl a-binding LHC by Add to
in vitro reconstitution: LHCaR1 binds 8 Chl a molecules and marked
proportionately more carotenoids than CAB proteins items
Journal Photosynthesis Research Add to
Publisher Springer Netherlands shopping
ISSN 0166-8595 (Print) 1573-5079 (Online) cart
Issue Volume 63, Number 1 / January, 2000 Add to
DOI 10.1023/A:1006357107247 saved items
Pages 85-96 Request
Subject Collection Biomedical and Life Sciences Permissions
SpringerLink DateTuesday, November 02, 2004 Recommend
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Characterization of the Porphyridium cruentum Chl a-binding LHC by Query Builder Close |
in vitro reconstitution: LHCaR1 binds 8 Chl a molecules and Clear
proportionately more carotenoids than CAB proteins
Title (ti)
Beatrice Grabowski 1 , Shi Tan1, 2 , Francis X. Cunningham Jr.1 and Summary (su)
3 Author (au)
Elisabeth Gantt
ISSN (issn)
ISBN (isbn)
(1) Department of Cell Biology and Molecular Genetics, University of
DOI (doi)
Maryland, College Park, MD 20742, USA
(2) Present address: Department of Physiology, University of
Massachusetts Medical School, Worcester, MA 01655, USA And
(3) Department of Cell Biology and Molecular Genetics, University of Or
Maryland, College Park, MD 20742, USA Not
Abstract The Porphyridium cruentum light harvesting complex (LHC) )
binds Chl a, zeaxanthin and -carotene and comprises at least 6 * (wildcard)
"" (exact)
polypeptides of a multigene family. We describe the first in vitro
reconstitution of a red algal light-harvesting protein (LHCaR1) with Within all content
Chl a/carotenoid extracts from P. cruentum. The reconstituted pigment Within this journal
complex (rLHCaR1) is spectrally similar to the native LHC I, with an Within this issue
absorption maximum at 670 nm, a 77 K fluorescence emission peak at Export this article
677 nm (ex. 440 nm), and similar circular dichroism spectra. Molar Export this article as RIS
ratios of 4.0 zeaxanthin, 0.3 -carotene and 8.2 Chl a per polypeptide | Text
for rLHCaR1 are similar to those of the native LHC I complex (3.1
zeaxanthin, 0.5 -carotene, 8.5 Chl a). The binding of 8 Chl a Text
molecules per apoprotein is consistent with 8 putative Chl-binding sites
in the predicted transmembrane helices of LHCaR1. Two of the PDF
putative Chl a binding sites (helix 2) in LHCaR1 were assigned to Chl
b in Chl a/b-binding (CAB) LHC II [Kühlbrandt et al. (1994) Nature The size of this document
367: 614–21]. This suggests either that discrimination for binding of is 325 kilobytes.
Chl a or Chl b is not very specific at these sites or that specificity of Although it may be a
binding sites evolved separately in CAB proteins. LHCaR1 can be lengthier download, this
reconstituted with varying ratios of carotenoids, consistent with our is the most authoritative
previous observation that the carotenoid to Chl ratio is substantially online format.
higher in P. cruentum grown under high irradiance. Also notable is that
zeaxanthin does not act as an accessory light-harvesting pigment, even Open: Entire document
though it is highly likely that it occupies the position assigned to lutein
in the CAB LHCs. HTML

chlorophyll a - Chl a-binding protein - evolution - light-harvesting This offers the quickest
complex - LHC I - Porphyridium cruentum - reconstitution - red alga - access for ease of
zeaxanthin browsing. Please note
that some scientific and
This revised version was published online in October 2005 with mathematical characters
corrections to the Cover Date. may not render as
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Elisabeth Gantt versions.
Fax: +1-301-314-9489 Open Full Text

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