Influence of the protein binding site on the excited states of bacteriochlorophyll: DFT calculations of B800 in LH2
(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)
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https://lup.lub.lu.se/record/324193
- author
- He, Zhi LU ; Sundström, Villy LU and Pullerits, Tönu LU
- organization
- publishing date
- 2002
- 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 (ACS)
- external identifiers
-
- wos:000179011500029
- scopus:0037038477
- ISSN
- 1520-5207
- DOI
- 10.1021/jp020063z
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Chemical Physics (S) (011001060)
- id
- 0d6d2d09-7a10-474a-9ffe-02183f5d4b3d (old id 324193)
- date added to LUP
- 2016-04-01 15:31:59
- date last changed
- 2022-01-28 05:49:03
@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 (ACS)}}, 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}}, doi = {{10.1021/jp020063z}}, volume = {{106}}, year = {{2002}}, }