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Cytochrome b(6)f: structure for signalling and vectorial metabolism

Allen, John LU (2004) In Trends in Plant Science 9(3). p.130-137
Abstract
Following decades of detailed kinetic and spectroscopic evidence, two new, independent X-ray structures for the cytochrome b(6)f complex of photosynthesis now reveal the arrangement of its key electron carriers relative to each other, and to their protein ligands. But these are not predictable additions to the structural collection. The complex is dimeric, and encloses a central chamber in which plastoquinone and its redox intermediates couple proton translocation with cytochrome oxidation and reduction. The structures also announce a fourth, wholly unexpected haem, that could be the long-sought, missing link of photosystem I cyclic photophosphorylation. One chlorophyll molecule and one carotenoid molecule add to the enigma of this dark,... (More)
Following decades of detailed kinetic and spectroscopic evidence, two new, independent X-ray structures for the cytochrome b(6)f complex of photosynthesis now reveal the arrangement of its key electron carriers relative to each other, and to their protein ligands. But these are not predictable additions to the structural collection. The complex is dimeric, and encloses a central chamber in which plastoquinone and its redox intermediates couple proton translocation with cytochrome oxidation and reduction. The structures also announce a fourth, wholly unexpected haem, that could be the long-sought, missing link of photosystem I cyclic photophosphorylation. One chlorophyll molecule and one carotenoid molecule add to the enigma of this dark, downhill electron transfer complex, linking the real photosystems I and II. Conserved structural features offer clues to the evolution of photosynthesis, and to the initiation of redox signals required for genome function. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Trends in Plant Science
volume
9
issue
3
pages
130 - 137
publisher
Elsevier
external identifiers
  • wos:000220461100006
  • pmid:15003236
  • scopus:1542321529
ISSN
1360-1385
DOI
10.1016/j.tplants.2004.01.009
language
English
LU publication?
yes
id
8881306b-6fb7-4a05-98da-a08cc110f9a8 (old id 138605)
date added to LUP
2007-07-04 09:42:49
date last changed
2017-10-01 03:52:44
@article{8881306b-6fb7-4a05-98da-a08cc110f9a8,
  abstract     = {Following decades of detailed kinetic and spectroscopic evidence, two new, independent X-ray structures for the cytochrome b(6)f complex of photosynthesis now reveal the arrangement of its key electron carriers relative to each other, and to their protein ligands. But these are not predictable additions to the structural collection. The complex is dimeric, and encloses a central chamber in which plastoquinone and its redox intermediates couple proton translocation with cytochrome oxidation and reduction. The structures also announce a fourth, wholly unexpected haem, that could be the long-sought, missing link of photosystem I cyclic photophosphorylation. One chlorophyll molecule and one carotenoid molecule add to the enigma of this dark, downhill electron transfer complex, linking the real photosystems I and II. Conserved structural features offer clues to the evolution of photosynthesis, and to the initiation of redox signals required for genome function.},
  author       = {Allen, John},
  issn         = {1360-1385},
  language     = {eng},
  number       = {3},
  pages        = {130--137},
  publisher    = {Elsevier},
  series       = {Trends in Plant Science},
  title        = {Cytochrome b(6)f: structure for signalling and vectorial metabolism},
  url          = {http://dx.doi.org/10.1016/j.tplants.2004.01.009},
  volume       = {9},
  year         = {2004},
}