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Rienk van Grondelle

Researcher at VU University Amsterdam

Publications -  479
Citations -  28979

Rienk van Grondelle is an academic researcher from VU University Amsterdam. The author has contributed to research in topics: Excited state & Photosynthetic reaction centre. The author has an hindex of 81, co-authored 476 publications receiving 26434 citations. Previous affiliations of Rienk van Grondelle include University of Sheffield & University of Chicago.

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Characterization of low-energy chlorophylls in the PSI-LHCI supercomplex from Chlamydomonas reinhardtii. A site-selective fluorescence study

TL;DR: It is demonstrated here that the low-energy pool of chlorophylls in the PSI-LHCI complex from the green alga Chlamydomonas reinhardtii, containing five to six pigments, is significantly blue-shifted (A(max) at 700 nm at 4 K) compared to that in thePSI core preparations from several species of cyanobacteria and in PSI's particles from higher plants.
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Different crystal morphologies lead to slightly different conformations of light-harvesting complex II as monitored by variations of the intrinsic fluorescence lifetime

TL;DR: Compared the fluorescence of various types of crystals, differing in morphology and age, which indicates that fluorescence is not quenched by random impurities and packing defects, but that LHCII adopts a particular structure in each crystal type, that leads to fluorescence quenching.
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The origin of the unusual Qy red shift in LH1-RC complexes from purple bacteria Thermochromatium tepidum as revealed by Stark absorption spectroscopy.

TL;DR: A combined effect of exciton-charge transfer states mixing, and inhomogeneous narrowing of the BChl a site energy is proposed to be the origin of the 915 nm absorption of native LH1-RC of photosynthetic purple bacteria Thermochromatium tepidum LH1.
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Impact of Photon Absorption on the Electronic Properties of p-Coumaric Acid Derivatives of the Photoactive Yellow Protein Chromophore

TL;DR: In this paper, the electrostatic properties of thiomethyl p-coumaric acid (TMpCA) and its sterically hindered derivative, THI7HC, were determined at 77 K using Stark spectroscopy, to better understand the origin of the photoinduced charge motion observed in these chromophores in the native photoactive yellow protein (PYP) environment.