Abstract
Rate constants for the primary photoinduced electron transfer reactions within the reaction center protein of the photosynthetic bacterium Rhodopseudomonas viridis have been measured using transient optical absorption spectroscopy following excitation of the primary donor P960 directly with 950 nm laser flashes. The time resolution of the experiments was 0.45 ps. The reduction of BPheo b as indicated by absorption changes at 543 nm exhibits monophasic kinetics with a 1.7 × 1011 s1̄ rate constant following direct excitation of P960. Spectral changes at 805 and 835 nm due to perturbations of the intermediary BChl b occur synchronously with those at 543 nm. There is no evidence for formation of BChl b- as a distinct chemical intermediate preceding the reduction of BPheo b.
| Original language | English |
|---|---|
| Pages (from-to) | 368-372 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 204 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Aug 18 1986 |
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Keywords
- Bacterial photosynthesis Charge separation Ultrafast spectroscopy
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Sub-picosecond measurements of primary electron transfer in Rhodopseudomonas viridis reaction centers using near-infrared excitation. / Wasielewski, Michael R; Tiede, David M.
In: FEBS Letters, Vol. 204, No. 2, 18.08.1986, p. 368-372.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Sub-picosecond measurements of primary electron transfer in Rhodopseudomonas viridis reaction centers using near-infrared excitation
AU - Wasielewski, Michael R
AU - Tiede, David M.
PY - 1986/8/18
Y1 - 1986/8/18
N2 - Rate constants for the primary photoinduced electron transfer reactions within the reaction center protein of the photosynthetic bacterium Rhodopseudomonas viridis have been measured using transient optical absorption spectroscopy following excitation of the primary donor P960 directly with 950 nm laser flashes. The time resolution of the experiments was 0.45 ps. The reduction of BPheo b as indicated by absorption changes at 543 nm exhibits monophasic kinetics with a 1.7 × 1011 s1̄ rate constant following direct excitation of P960. Spectral changes at 805 and 835 nm due to perturbations of the intermediary BChl b occur synchronously with those at 543 nm. There is no evidence for formation of BChl b- as a distinct chemical intermediate preceding the reduction of BPheo b.
AB - Rate constants for the primary photoinduced electron transfer reactions within the reaction center protein of the photosynthetic bacterium Rhodopseudomonas viridis have been measured using transient optical absorption spectroscopy following excitation of the primary donor P960 directly with 950 nm laser flashes. The time resolution of the experiments was 0.45 ps. The reduction of BPheo b as indicated by absorption changes at 543 nm exhibits monophasic kinetics with a 1.7 × 1011 s1̄ rate constant following direct excitation of P960. Spectral changes at 805 and 835 nm due to perturbations of the intermediary BChl b occur synchronously with those at 543 nm. There is no evidence for formation of BChl b- as a distinct chemical intermediate preceding the reduction of BPheo b.
KW - Bacterial photosynthesis Charge separation Ultrafast spectroscopy
UR - http://www.scopus.com/inward/record.url?scp=0342693639&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0342693639&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(86)80845-6
DO - 10.1016/0014-5793(86)80845-6
M3 - Article
VL - 204
SP - 368
EP - 372
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 2
ER -