Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Low-temperature spectroscopy of fully active cores. Comparison with CP43, CP47,

Peterson Årsköld, Sindra LU ; Prince, Barry J ; Krausz, Elmars ; Smith, Paul ; Pace, Ron J ; Picorel, Rafael and Seibert, Mikael (2004) In Journal of Luminescence 108(1-4). p.97-100
Abstract
Comparisons of absorption spectra of photosystem II (PSII) core complexes with those of isolated CP43, CP47 and D1/D2/cyt b559 complexes show broadenings and shifts upon disassembly of the PSII core material. Spectra of PSII cores isolated from plants and cyanobacteria reveal marked changes in energies and intensities of the sharp features associated with P680. Low-temperature, illumination-induced electrochromic shifts in PSII cores allow identification of an excitation localized on pheopytin-a (pheo a) in D1. A weak interaction between an exciton component of P680 and the D1 pheo a, both located near 684 nm, is suggested. MCD spectra of 5- and 6-chlorophyll a D1/D2/cytochrome b559 preparations provide links to photoactive pigments in... (More)
Comparisons of absorption spectra of photosystem II (PSII) core complexes with those of isolated CP43, CP47 and D1/D2/cyt b559 complexes show broadenings and shifts upon disassembly of the PSII core material. Spectra of PSII cores isolated from plants and cyanobacteria reveal marked changes in energies and intensities of the sharp features associated with P680. Low-temperature, illumination-induced electrochromic shifts in PSII cores allow identification of an excitation localized on pheopytin-a (pheo a) in D1. A weak interaction between an exciton component of P680 and the D1 pheo a, both located near 684 nm, is suggested. MCD spectra of 5- and 6-chlorophyll a D1/D2/cytochrome b559 preparations provide links to photoactive pigments in intact PSII cores. (Less)
Please use this url to cite or link to this publication:
author
; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
STARK SHIFTS, RESOLUTION, REACTION CENTERS, PHOTOSYSTEM-II, CRYSTAL-STRUCTURE, PROTEIN, PIGMENTS, COMPLEXES
in
Journal of Luminescence
volume
108
issue
1-4
pages
97 - 100
publisher
Elsevier
external identifiers
  • scopus:2342544879
ISSN
0022-2313
DOI
10.1016/j.jlumin.2004.01.023
language
English
LU publication?
yes
id
ef2094dd-18ef-4075-ba11-a161229c2b62 (old id 120915)
date added to LUP
2016-04-01 16:39:50
date last changed
2022-01-28 21:17:38
@article{ef2094dd-18ef-4075-ba11-a161229c2b62,
  abstract     = {{Comparisons of absorption spectra of photosystem II (PSII) core complexes with those of isolated CP43, CP47 and D1/D2/cyt b559 complexes show broadenings and shifts upon disassembly of the PSII core material. Spectra of PSII cores isolated from plants and cyanobacteria reveal marked changes in energies and intensities of the sharp features associated with P680. Low-temperature, illumination-induced electrochromic shifts in PSII cores allow identification of an excitation localized on pheopytin-a (pheo a) in D1. A weak interaction between an exciton component of P680 and the D1 pheo a, both located near 684 nm, is suggested. MCD spectra of 5- and 6-chlorophyll a D1/D2/cytochrome b559 preparations provide links to photoactive pigments in intact PSII cores.}},
  author       = {{Peterson Årsköld, Sindra and Prince, Barry J and Krausz, Elmars and Smith, Paul and Pace, Ron J and Picorel, Rafael and Seibert, Mikael}},
  issn         = {{0022-2313}},
  keywords     = {{STARK SHIFTS; RESOLUTION; REACTION CENTERS; PHOTOSYSTEM-II; CRYSTAL-STRUCTURE; PROTEIN; PIGMENTS; COMPLEXES}},
  language     = {{eng}},
  number       = {{1-4}},
  pages        = {{97--100}},
  publisher    = {{Elsevier}},
  series       = {{Journal of Luminescence}},
  title        = {{Low-temperature spectroscopy of fully active cores. Comparison with CP43, CP47,}},
  url          = {{http://dx.doi.org/10.1016/j.jlumin.2004.01.023}},
  doi          = {{10.1016/j.jlumin.2004.01.023}},
  volume       = {{108}},
  year         = {{2004}},
}