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Featured researches published by S. D'Haene.


Biophysical Journal | 2009

A Mechanism of Energy Dissipation in Cyanobacteria

Rudi Berera; Ivo H. M. van Stokkum; S. D'Haene; John T. M. Kennis; Rienk van Grondelle; Jan P. Dekker

When grown under a variety of stress conditions, cyanobacteria express the isiA gene, which encodes the IsiA pigment-protein complex. Overexpression of the isiA gene under iron-depletion stress conditions leads to the formation of large IsiA aggregates, which display remarkably short fluorescence lifetimes and thus a strong capacity to dissipate energy. In this work we investigate the underlying molecular mechanism responsible for chlorophyll fluorescence quenching. Femtosecond transient absorption spectroscopy allowed us to follow the process of energy dissipation in real time. The light energy harvested by chlorophyll pigments migrated within the system and eventually reaches a quenching site where the energy is transferred to a carotenoid-excited state, which dissipates it by decaying to the ground state. We compare these findings with those obtained for the main light-harvesting complex in green plants (light-harvesting complex II) and artificial light-harvesting antennas, and conclude that all of these systems show the same mechanism of energy dissipation, i.e., one or more carotenoids act as energy dissipators by accepting energy via low-lying singlet-excited S(1) states and dissipating it as heat.


Biochimica et Biophysica Acta | 2015

Identification of common motifs in the regulation of light harvesting: The case of cyanobacteria IsiA.

Md. Wahadoszamen; S. D'Haene; Anjue Mane Ara; Elisabet Romero; Jan P. Dekker; Rienk van Grondelle; Rudi Berera

When cyanobacteria are grown under iron-limited or other oxidative stress conditions the iron stress inducible pigment-protein IsiA is synthesized in variable amounts. IsiA accumulates in aggregates inside the photosynthetic membrane that strongly dissipate chlorophyll excited state energy. In this paper we applied Stark fluorescence (SF) spectroscopy at 77K to IsiA aggregates to gain insight into the nature of the emitting and energy dissipating state(s). Our study shows that two emitting states are present in the system, one emitting at 684 nm and the other emitting at about 730 nm. The new 730 nm state exhibits strongly reduced fluorescence (F) together with a large charge transfer character. We discuss these findings in the light of the energy dissipation mechanisms involved in the regulation of photosynthesis in plants, cyanobacteria and diatoms. Our results suggest that photosynthetic organisms have adopted common mechanisms to cope with the deleterious effects of excess light under unfavorable growth conditions.


Biochimica et Biophysica Acta | 2014

Organization in photosynthetic membranes of purple bacteria in vivo: The role of carotenoids

S. D'Haene; Lucy I. Crouch; Michael R. Jones; Raoul N. Frese

Photosynthesis in purple bacteria is performed by pigment-protein complexes that are closely packed within specialized intracytoplasmic membranes. Here we report on the influence of carotenoid composition on the organization of RC-LH1 pigment-protein complexes in intact membranes and cells of Rhodobacter sphaeroides. Mostly dimeric RC-LH1 complexes could be isolated from strains expressing native brown carotenoids when grown under illuminated/anaerobic conditions, or from strains expressing green carotenoids when grown under either illuminated/anaerobic or dark/semiaerobic conditions. However, mostly monomeric RC-LH1 complexes were isolated from strains expressing the native photoprotective red carotenoid spheroidenone, which is synthesized during phototrophic growth in the presence of oxygen. Despite this marked difference, linear dichroism (LD) and light-minus-dark LD spectra of oriented intact intracytoplasmic membranes indicated that RC-LH1 complexes are always assembled in ordered arrays, irrespective of variations in the relative amounts of isolated dimeric and monomeric RC-LH1 complexes. We propose that part of the photoprotective response to the presence of oxygen mediated by synthesis of spheroidenone may be a switch of the structure of the RC-LH1 complex from dimers to monomers, but that these monomers are still organized into the photosynthetic membrane in ordered arrays. When levels of the dimeric RC-LH1 complex were very high, and in the absence of LH2, LD and ∆LD spectra from intact cells indicated an ordered arrangement of RC-LH1 complexes. Such a degree of ordering implies the presence of highly elongated, tubular membranes with dimensions requiring orientation along the length of the cell and in a proportion larger than previously observed.


Biochemistry | 2004

Supramolecular organization and dual function of the IsiA chlorophyll-binding protein in cyanobacteria

Nataliya Yeremenko; Roman Kouril; J.A. Ihalainen; S. D'Haene; N. van Oosterwijk; Elena G. Andrizhiyevskaya; Wilko Keegstra; H.L. Dekker; M. Hagemann; Egbert J. Boekema; H.C.P. Matthijs; Jan P. Dekker; Sandrine D’Haene


Biochemistry | 2005

Aggregates of the chlorophyll-binding protein IsiA (CP43 ') dissipate energy in cyanobacteria

J.A. Ihalainen; S. D'Haene; Nataliya Yeremenko; H van Roon; Ana A. Arteni; Egbert J. Boekema; R. van Grondelle; H.C.P. Matthijs; Jan P. Dekker; Sandrine D’Haene


Biochimica et Biophysica Acta | 2002

Spectroscopic properties of PSI-IsiA supercomplexes from the cyanobacterium Synechococcus PCC 7942

Elena G. Andrizhiyevskaya; Tatjana Martha Edith Schwabe; Marta Germano; S. D'Haene; Jochen Kruip; Rienk van Grondelle; Jan P. Dekker


Biochimica et Biophysica Acta | 2003

Photosystem I trimers from Synechocystis PCC 6803 lacking the PsaF and PsaJ subunits bind an IsiA ring of 17 units

Roman Kouril; Nataliya Yeremenko; S. D'Haene; Alevtyna E. Yakushevska; Wilko Keegstra; H.C.P. Matthijs; Jan P. Dekker; Egbert J. Boekema


Biochimica et Biophysica Acta | 2015

Interaction of the PsbH subunit with a chlorophyll bound to histidine 114 of CP47 is responsible for the red 77 K fluorescence of Photosystem II

S. D'Haene; Roman Sobotka; Lenka Bučinská; Jan P. Dekker; Josef Komenda


Biochimica et Biophysica Acta | 2005

Supercomplexes of IsiA and Photosystem I in a mutant lacking subunit PsaL

Roman Kouril; Nataliya Yeremenko; S. D'Haene; Gert T. Oostergetel; H.C.P. Matthijs; Jan P. Dekker; Egbert J. Boekema


Biochimica et Biophysica Acta | 2007

Fluorescence quenching of IsiA in early stage of iron deficiency and at cryogenic temperatures

Chantal D. van der Weij-de Wit; J.A. Ihalainen; Edith van de Vijver; S. D'Haene; H.C.P. Matthijs; Rienk van Grondelle; Jan P. Dekker

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Roman Kouril

University of Groningen

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Rudi Berera

VU University Amsterdam

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