Energy transfer and bacteriochlorophyll fluorescence in purple bacteria at low temperature

Rijgersberg, C.P.; Grondelle, Rienk van; Amesz, J.

doi:10.1016/0005-2728(80)90113-9

Cited by 69 publications

(39 citation statements)

References 21 publications

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“…Kinetics measured as a function of temperature show that the trapping time constant for R. rubrum increases from about 40 ps at 100 K to 75 ps at 77 K observed here [13], whereas for Rb. sphaeroides it remains constant (37 ps) over the entire temperature interval of 177-77 K. Previous measurements of the temperature dependence of the fluorescence quantum yield [14] have shown that the fluore- From the schemes above it is evident that the final trapping step occurs with a rate typical of other inter-complex energy-transfer processes in purple bacteria. The time constant of this step is of the same order of magnitude as the total trapping time observed at room temperature [1].…”

Section: Resultsmentioning

confidence: 85%

Characterization of excitation energy trapping in photosynthetic purple bacteria at 77 K

1989

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We have studied the energy-transfer dynamics in chromatophores of Rhodobacter sphaeroides and Rhodospirillum rubrum at 77 K, with functional charge separation. Using low-intensity picosecond absorption recovery, we determined that transfer between the energetically low-lying antenna component BCh1896 and the special pair of the reaction center occurs with a time constant of 37 ps in Rb. sphaeroides and 75 ps in R. rubrum. Assuming that a F6rster energy-transfer mechanism applies to the process, this allows us to estimate the distance between BCh1896 in the B875 complex and the special pair P870 in the reaction center to range between 26 and 39/~, in Rb. sphaeroides. Such a distance indicates that the BChI896 pigment and the special pair of the reaction center are at the minimum separation allowed by the size and shape of the reaction center and the light-harvesting polypeptides.

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Section: Resultsmentioning

confidence: 85%

Characterization of excitation energy trapping in photosynthetic purple bacteria at 77 K

1989

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“…There are indeed several observations that peripheral antenna do fluoresce: an emission from the peripheral antenna of Rhodopseudomonas sphaeroides (BSOO-850) has been detected in the FO (but not in the Fv) spectrum at room temperature [19,36]. A specific contribution of FssO, the emission from LHC, to the FO spectrum of chloroplasts has been reported at 4 K [19].…”

Section: Discussionmentioning

confidence: 99%

The emission of chlorophyll in vivo

Breton¹

1983

FEBS Letters

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Low temperature photosystem 2 emission (Fans, F695) of chloroplasts may originate from a Snd pool of pigments. However, the excitons reaching the reaction center have been generated in a much larger pool of chIorophylls constituting the almost non-~uorescent iight-h~vesti~ complex. Based upon structural info~ation an interpretation for the mOhXUhU Origin Of the F695 emission Of variable yield was proposed [FEBS Lett. (1982) 147, 17-201: in reaction centers having the quinone acceptor reduced, a charge recombination occurring between the primary donor P680+ and Phe-(the pheophytin primary acceptor) can generate a singlet excited state of Phe which deactivates by emitting F695. Here, an analogous process is discussed for F685 with the emission occurring either from P680 directly or from the small pool of core antenna chlorophylls surrounding the reaction center. Furthermore, the presence of F695 in the low temperature emission spectra of dark-adapted chioropl~ts leads us to propose that charge recombination also takes place in open reaction centers when the quinone acceptor is oxidized. In this case the short lifetime (130 f 20 ps) observed for the singlet exciton in the intact membrane suggests that the rate-limiting step in conditions of active photosynthesis is more probably determined by the stabilization of the negative charge on the quinone than by either the rate of energy transfer among antenna or the rate of trapping by the reaction center. Primary reaction Photosystem 2 Low temperature fluorescence Charge recombination luminescenceEnergy transfer

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“…They demonstrated that this blue-shifted strain, designated R26.1, contained not only LH1 but also an altered LH2 complex, in which the B800 peak is absent. This explained earlier spectroscopic observations that R26.1 contains two types of antenna complex (for example, Rijgersberg et al, 1980) and this was confirmed by subsequent work (Robert et al, 1984). Theiler et al (1985) determined the amino acid sequence of the LH1 polypeptides from R26.1 and a comparison with the wild type LH1 revealed a which was proposed to weaken the heterodimer.…”

Section: R26 and R261supporting

confidence: 73%

Genetic Manipulation of the Antenna Complexes of Purple Bacteria

Hunter

Advances in Photosynthesis and Respiration

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Energy transfer and bacteriochlorophyll fluorescence in purple bacteria at low temperature

Cited by 69 publications

References 21 publications

Characterization of excitation energy trapping in photosynthetic purple bacteria at 77 K

Characterization of excitation energy trapping in photosynthetic purple bacteria at 77 K

The emission of chlorophyll in vivo

Genetic Manipulation of the Antenna Complexes of Purple Bacteria

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