Energy transfer in the peridinin-chicrophyll protein complex reconstituted with mixed chlorophyll sites
(2008) In Biophysical Journal 94(8). p.3198-3207- Abstract
- We use femtosecond transient absorption spectroscopy to study chlorophyll (Chl)-Chl energy transfer in the peridinin-chlorophyll protein (PCP) reconstituted with mixtures of either chlorophyll b (Chlb) and Chld or Chla and bacteriochlorophyll a (BChla). Analysis of absorption and transient absorption spectra demonstrated that reconstitution with chlorophyll mixtures produces a significant fraction of PCP complexes that contains a different Chl in each domain of the PCP monomer. The data also suggest that binding affinity of Chla is less than that of the other three Chl species. By exciting the Chl species lying at higher energy, we obtained energy transfer times of 40 +/- 5 ps (Chlb-Chld) and 59 3 ps (Chla-BChla). The experimental values... (More)
- We use femtosecond transient absorption spectroscopy to study chlorophyll (Chl)-Chl energy transfer in the peridinin-chlorophyll protein (PCP) reconstituted with mixtures of either chlorophyll b (Chlb) and Chld or Chla and bacteriochlorophyll a (BChla). Analysis of absorption and transient absorption spectra demonstrated that reconstitution with chlorophyll mixtures produces a significant fraction of PCP complexes that contains a different Chl in each domain of the PCP monomer. The data also suggest that binding affinity of Chla is less than that of the other three Chl species. By exciting the Chl species lying at higher energy, we obtained energy transfer times of 40 +/- 5 ps (Chlb-Chld) and 59 3 ps (Chla-BChla). The experimental values match those obtained from the Forster equation, 36 and 50 ps, respectively, showing that energy transfer proceeds via the Forster mechanism. Excitation of peridinin in the PCP complex reconstituted with Chla/BChla mixture provided time constants of 2.6 and 0.4 ps for the peridinin-Chla and peridinin-BChla energy transfer, matching those obtained from studies of PCP complexes reconstituted with single chlorophyll species. (Less)
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https://lup.lub.lu.se/record/1183044
- author
- Polivka, Tomas ; Pascher, Torbjörn LU and Hiller, Roger G
- organization
- publishing date
- 2008
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biophysical Journal
- volume
- 94
- issue
- 8
- pages
- 3198 - 3207
- publisher
- Cell Press
- external identifiers
-
- wos:000254420100028
- scopus:43149098310
- ISSN
- 1542-0086
- DOI
- 10.1529/biophysj.107.123430
- 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
- e0bce95c-8a06-421f-a56a-82886eb16180 (old id 1183044)
- date added to LUP
- 2016-04-01 12:12:11
- date last changed
- 2022-01-27 00:21:51
@article{e0bce95c-8a06-421f-a56a-82886eb16180,
abstract = {{We use femtosecond transient absorption spectroscopy to study chlorophyll (Chl)-Chl energy transfer in the peridinin-chlorophyll protein (PCP) reconstituted with mixtures of either chlorophyll b (Chlb) and Chld or Chla and bacteriochlorophyll a (BChla). Analysis of absorption and transient absorption spectra demonstrated that reconstitution with chlorophyll mixtures produces a significant fraction of PCP complexes that contains a different Chl in each domain of the PCP monomer. The data also suggest that binding affinity of Chla is less than that of the other three Chl species. By exciting the Chl species lying at higher energy, we obtained energy transfer times of 40 +/- 5 ps (Chlb-Chld) and 59 3 ps (Chla-BChla). The experimental values match those obtained from the Forster equation, 36 and 50 ps, respectively, showing that energy transfer proceeds via the Forster mechanism. Excitation of peridinin in the PCP complex reconstituted with Chla/BChla mixture provided time constants of 2.6 and 0.4 ps for the peridinin-Chla and peridinin-BChla energy transfer, matching those obtained from studies of PCP complexes reconstituted with single chlorophyll species.}},
author = {{Polivka, Tomas and Pascher, Torbjörn and Hiller, Roger G}},
issn = {{1542-0086}},
language = {{eng}},
number = {{8}},
pages = {{3198--3207}},
publisher = {{Cell Press}},
series = {{Biophysical Journal}},
title = {{Energy transfer in the peridinin-chicrophyll protein complex reconstituted with mixed chlorophyll sites}},
url = {{http://dx.doi.org/10.1529/biophysj.107.123430}},
doi = {{10.1529/biophysj.107.123430}},
volume = {{94}},
year = {{2008}},
}