Temperature dependence of energy transfer from the long wavelength antenna BChl-896 to the reaction center in Rhodospirillum rubrum, Rhodobacter sphaeroides (w.t. and M21 mutant) from 77 to 177K, studied by picosecond absorption spectroscopy

Visscher, K.J.; Bergström, Hans; Sundström, Villy; Hunter, C. Neil; Grondelle, Rienk van

doi:10.1007/bf00048300

Cited by 102 publications

(68 citation statements)

References 25 publications

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“…Exciton-based excitation transfer in the chromatophore proceeds within 10-100 ps , first among the LH2s, then from LH2 to LH1, and finally from LH1 to the four BChls of the RC (Visscher et al, 1989;Beekman et al, 1994;Strümpfer and Schulten, 2012a;Sener et al, 2009). In the RC, the excitation quickly settles onto the so-called special pair BChls (Small, 1995;Damjanovic´et al, 2000), where it induces the transfer of an electron (Pawlowicz et al, 2008;Jordanides et al, 2004).…”

Section: Stage I: Light Absorption Excitation Energy Transfer and Qmentioning

confidence: 99%

“…For reviews see (van Grondelle and Novoderezhkin, 2006a;Sener et al, 2011;Strümpfer et al, 2012). Excitation transfer kinetics in the chromatophore was reported experimentally in (Woodbury and Parson, 1984;Visscher et al, 1989;Crielaard et al, 1994;Hess et al, 1994Hess et al, , 1995. Exciton migration across the network of light harvesting complexes in the chromatophore can be described by a rate matrix K which is constructed from inter-complex exciton transfer rates k IJ , the latter given by Equation (S6), as follows (Sener et al, 2010(Sener et al, , 2007 …”

Section: Stage I: Light Absorption Excitation Energy Transfer and Qmentioning

confidence: 99%

“…The functional principles displayed by the chromatophore and prevalent also in other photosynthetic systems include efficient excitonic coupling between components (Hu et al, 1997van Grondelle and Novoderezhkin, 2006b;Olaya-Castro et al, 2008;Sener et al, 2011), the utilization of quantum coherence (Ishizaki and Fleming, 2009a;Strümpfer et al, 2012), photoprotection by carotenoids (Damjanovic´et al, 1999), accommodation of thermal fluctuations, studied through experimental (Visscher et al, 1989;van Grondelle et al, 1994;Pullerits et al, 1994;Gobets et al, 2001;Janusonis et al, 2008;Freiberg et al, 2009) as well as theoretical (Damjanovic´et al, 2002;Ishizaki and Fleming, 2009b; van Grondelle eLife digest Photosynthesis, or the conversion of light energy into chemical energy, is a process that powers almost all life on Earth. Plants and certain bacteria share similar processes to perform photosynthesis, though the purple bacterium Rhodobacter sphaeroides uses a photosynthetic system that is much less complex than that in plants.…”

Section: Introductionmentioning

confidence: 99%

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Overall energy conversion efficiency of a photosynthetic vesicle

Sener

Strümpfer

Singharoy

et al. 2016

eLife

174

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The chromatophore of purple bacteria is an intracellular spherical vesicle that exists in numerous copies in the cell and that efficiently converts sunlight into ATP synthesis, operating typically under low light conditions. Building on an atomic-level structural model of a low-lightadapted chromatophore vesicle from Rhodobacter sphaeroides, we investigate the cooperation between more than a hundred protein complexes in the vesicle. The steady-state ATP production rate as a function of incident light intensity is determined after identifying quinol turnover at the cytochrome bc 1 complex (cytbc 1 ) as rate limiting and assuming that the quinone/quinol pool of about 900 molecules acts in a quasi-stationary state. For an illumination condition equivalent to 1% of full sunlight, the vesicle exhibits an ATP production rate of 82 ATP molecules/s. The energy conversion efficiency of ATP synthesis at illuminations corresponding to 1%-5% of full sunlight is calculated to be 0.12-0.04, respectively. The vesicle stoichiometry, evolutionarily adapted to the low light intensities in the habitat of purple bacteria, is suboptimal for steady-state ATP turnover for the benefit of protection against over-illumination.

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Section: Stage I: Light Absorption Excitation Energy Transfer and Qmentioning

confidence: 99%

Section: Stage I: Light Absorption Excitation Energy Transfer and Qmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Overall energy conversion efficiency of a photosynthetic vesicle

Sener

Strümpfer

Singharoy

et al. 2016

eLife

174

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“…This particular energy transfer step, which takes ϳ35-45 ps (3), is important, because it is the rate-limiting step in the process of trapping light energy in photosynthetic bacteria (4).…”

mentioning

confidence: 99%

Structural Analysis of the Reaction Center Light-harvesting Complex I Photosynthetic Core Complex of Rhodospirillum rubrum Using Atomic Force Microscopy

Fotiadis

Qian

Philippsen

et al. 2004

Journal of Biological Chemistry

147

123

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The bacterium Rhodospirillum rubrum contains a simple photosynthetic system, in which the reaction center (RC) receives energy from the light-harvesting (LH1) complex. We have used high-resolution atomic force microscopy (AFM) to image two-dimensional crystals of the RC-LH1 complex of R. rubrum. The AFM topographs show that the RC-LH1 complex is ϳ94 Å in height, the RC-H subunit protrudes from the cytoplasmic face of the membrane by 40 Å, and it sits 21 Å above the highest point of the surrounding LH1 ring. In contrast, the RC on the periplasmic side is at a lower level than LH1, which protrudes from the membrane by 12 Å. The RC-LH1 complex can adopt an irregular shape in regions of uneven packing forces in the crystal; this reflects a likely flexibility in the natural membrane, which might be functionally important by allowing the export of quinol formed as a result of RC photochemistry. Nanodissection of the RC by the AFM tip removes the RC-H subunit and reveals the underlying RC-L and -M subunits. LH1 complexes completely lacking the RC were also found, providing ideal conditions for imaging both rings of LH1 polypeptides for the first time by AFM. In addition, we demonstrate the ellipticity of the LH1 ring at the cytoplasmic and periplasmic sides of the membrane, in both the presence and absence of the RC. These AFM measurements have been reconciled with previous electron microscopy and NMR data to produce a model of the RC-LH1 complex.Photosynthetic organisms harvest light energy and convert it to a chemically useful form, using light-harvesting (LH) 1 and reaction center (RC) complexes. This coupling between LH and RC complexes involves close physical proximity because of the distance term governing energy transfer between the complexes (1). In the purple photosynthetic bacteria, the reaction center receives energy from the LH1 complex (reviewed in Ref.2). This particular energy transfer step, which takes ϳ35-45 ps (3), is important, because it is the rate-limiting step in the process of trapping light energy in photosynthetic bacteria (4).In view of the value of the RC-LH1 complex as a model for coupled light-harvesting energy transfer and photochemistry, structural information on the association between LH1 and RC complexes is required. Rhodospirillum rubrum, which represents one of the simplest possible photosynthetic systems, is valuable in this respect. A recent cryo-electron microscopy (EM) study of the RC-LH1 complex of R. rubrum, which built upon earlier work on the LH1-only (no RC) complex (5), shows that the RC complex is surrounded by a ring of 16␣ and 16␤ LH1 subunits, which would correspond to 32 bacteriochlorophylls (BChls) (6). This structure provides a rationale for the rate-limiting energy transfer step, because the ϳ45 Å distance from LH1 BChls to the special pair BChls of the RC is considerable (5, 6). This should be viewed in the context of known energy transfer steps and distances in these bacteria: for example, the internal transfer of energy in ϳ0.5-1 ps between the B800 and B850 BCh...

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“…1 Both the energy transfer and the energy trapping times for the reaction center have been reported to decrease at lower temperatures. 47,[63][64][65] The samples used in the APE measurements had open reaction centers at room temperature when not pumped by light. However, all the APE experiments were performed at low temperatures with unflowed samples and a laser pulse repetition rate of 94 MHz at 50 µW.…”

Section: Discussionmentioning

confidence: 99%

Exciton Dynamics in LH1 and LH2 of Rhodopseudomonas Acidophila and Rhodobium Marinum Probed with Accumulated Photon Echo and Pump−Probe Measurements

et al. 2000

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Exciton dynamics in the B850 and B875 bands of isolated complexes of Rhodopseudomonas acidophila (strain 10 050 and 7050) and in the B875 band of isolated complexes of Rhodobium marinum were investigated by means of accumulated photon echo and pump-probe techniques at different temperatures and wavelengths. For all three systems, the optical dephasing time T 2 was found to be very similar: at 4.2 K, T 2 is 116 and 106 ps for the B850 and B875 bands of Rhodopseudomonas acidophila, respectively, and 93 ps for the B875 band of Rhodobium marinum. The rapid dephasing, which displays glassy character, is a consequence of the strong pigment-protein interactions that arise through the rather short distances in these complexes. The observed dephasing time at the red edge of the B850 band of Rhodopseudomonas acidophila at 4.2 K reveals the existence of spectral diffusion in this system. From the wavelength dependence of the pump-probe signal in the B875 LH1 band of Rhodopseudomonas acidophila at 3 K it is concluded that energy transfer between energetically inequivalent LH1 rings occurs on a time scale of several tens picoseconds, while energy trapping takes place in about 250 ps.

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Temperature dependence of energy transfer from the long wavelength antenna BChl-896 to the reaction center in Rhodospirillum rubrum, Rhodobacter sphaeroides (w.t. and M21 mutant) from 77 to 177K, studied by picosecond absorption spectroscopy

Cited by 102 publications

References 25 publications

Overall energy conversion efficiency of a photosynthetic vesicle

Overall energy conversion efficiency of a photosynthetic vesicle

Structural Analysis of the Reaction Center Light-harvesting Complex I Photosynthetic Core Complex of Rhodospirillum rubrum Using Atomic Force Microscopy

Exciton Dynamics in LH1 and LH2 of Rhodopseudomonas Acidophila and Rhodobium Marinum Probed with Accumulated Photon Echo and Pump−Probe Measurements

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