Advanced

Influence of the protein binding site on the excited states of bacteriochlorophyll: DFT calculations of B800 in LH2

He, Zhi LU ; Sundström, Villy LU and Pullerits, Tönu LU (2002) In The Journal of Physical Chemistry Part B 106(44). p.11606-11612
Abstract
Effects of hydrogen bonding and the axial ligand interaction on the B800 band in two LH2 complexes Rhodopseudomonas (Rps.) acidophila and Rhodospirillum (Rs.) molischianum have been theo retically investigated by using density functional theory. The local electrostatic environment of the B800 bacteriochlorophyll is simulated as an atomic charge field consisting of the pigments in the protomer unit. Despite the fact that the B800 binding sites in two structures are very different, their absorption spectra are almost identical. Our calculations indicate that the charged axial ligand in Rs. molischianum and the hydrogen bonding in Rps. acidophila lead to similar red shifts, possibly explaining the above controversy. We also found (i)... (More)
Effects of hydrogen bonding and the axial ligand interaction on the B800 band in two LH2 complexes Rhodopseudomonas (Rps.) acidophila and Rhodospirillum (Rs.) molischianum have been theo retically investigated by using density functional theory. The local electrostatic environment of the B800 bacteriochlorophyll is simulated as an atomic charge field consisting of the pigments in the protomer unit. Despite the fact that the B800 binding sites in two structures are very different, their absorption spectra are almost identical. Our calculations indicate that the charged axial ligand in Rs. molischianum and the hydrogen bonding in Rps. acidophila lead to similar red shifts, possibly explaining the above controversy. We also found (i) additional B800 bacteriochlorophyll transitions located between the Q and Soret regions for both LH2 complexes and (ii) the ligand to the B800 charge-transfer excited states in the long-wavelength region for the B800-alphaAsp(6) complex in,the Rs. molischianum LH2 system. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
The Journal of Physical Chemistry Part B
volume
106
issue
44
pages
11606 - 11612
publisher
The American Chemical Society
external identifiers
  • wos:000179011500029
  • scopus:0037038477
ISSN
1520-5207
DOI
10.1021/jp020063z
language
English
LU publication?
yes
id
0d6d2d09-7a10-474a-9ffe-02183f5d4b3d (old id 324193)
date added to LUP
2007-10-15 08:57:09
date last changed
2017-02-12 04:02:34
@article{0d6d2d09-7a10-474a-9ffe-02183f5d4b3d,
  abstract     = {Effects of hydrogen bonding and the axial ligand interaction on the B800 band in two LH2 complexes Rhodopseudomonas (Rps.) acidophila and Rhodospirillum (Rs.) molischianum have been theo retically investigated by using density functional theory. The local electrostatic environment of the B800 bacteriochlorophyll is simulated as an atomic charge field consisting of the pigments in the protomer unit. Despite the fact that the B800 binding sites in two structures are very different, their absorption spectra are almost identical. Our calculations indicate that the charged axial ligand in Rs. molischianum and the hydrogen bonding in Rps. acidophila lead to similar red shifts, possibly explaining the above controversy. We also found (i) additional B800 bacteriochlorophyll transitions located between the Q and Soret regions for both LH2 complexes and (ii) the ligand to the B800 charge-transfer excited states in the long-wavelength region for the B800-alphaAsp(6) complex in,the Rs. molischianum LH2 system.},
  author       = {He, Zhi and Sundström, Villy and Pullerits, Tönu},
  issn         = {1520-5207},
  language     = {eng},
  number       = {44},
  pages        = {11606--11612},
  publisher    = {The American Chemical Society},
  series       = {The Journal of Physical Chemistry Part B},
  title        = {Influence of the protein binding site on the excited states of bacteriochlorophyll: DFT calculations of B800 in LH2},
  url          = {http://dx.doi.org/10.1021/jp020063z},
  volume       = {106},
  year         = {2002},
}