@article{LandauLoksteinSchelleretal.2009, author = {Landau, Alejandra Mabel and Lokstein, Heiko and Scheller, Henrik Vibe and Lainez, Veronica and Maldonado, Sara and Prina, Alberto Ra{\´u}l}, title = {A cytoplasmically inherited barley mutant is defective in photosystem I assembly due to a temperature-sensitive defect in ycf3 splicing}, issn = {0032-0889}, doi = {10.1104/pp.109.147843}, year = {2009}, abstract = {A cytoplasmically inherited chlorophyll-deficient mutant of barley (Hordeum vulgare) termed cytoplasmic line 3 (CL3), displaying a viridis (homogeneously light-green colored) phenotype, has been previously shown to be affected by elevated temperatures. In this article, biochemical, biophysical, and molecular approaches were used to study the CL3 mutant under different temperature and light conditions. The results lead to the conclusion that an impaired assembly of photosystem I (PSI) under higher temperatures and certain light conditions is the primary cause of the CL3 phenotype. Compromised splicing of ycf3 transcripts, particularly at elevated temperature, resulting from a mutation in a noncoding region (intron 1) in the mutant ycf3 gene results in a defective synthesis of Ycf3, which is a chaperone involved in PSI assembly. The defective PSI assembly causes severe photoinhibition and degradation of PSII.}, language = {en} } @article{MikhailyukLoksteinRazjivin2005, author = {Mikhailyuk, Igor K. and Lokstein, Heiko and Razjivin, Andrei P.}, title = {A method of spectral subband decomposition by simultaneous fitting the initial spectrum and a set of its derivatives}, year = {2005}, abstract = {An improved method for spectral subband decomposition based on simultaneous fitting of the initial spectrum and a set of its derivatives is introduced. Additionally, it procedure for finding an optimal smoothing filter to obtain undistorted derivatives IS Suggested. The proposed method is demonstrated with a model spectrum as well its with experimental absorption spectra of the photosynthetic antenna complexes, peridinin-chlorophyll a-protein (PCP) and the main light-harvesting complex of higher plants (LHC II). (c) 2005 Elsevier B.V. All rights reserved}, language = {en} } @article{EbenhoehHouwaartLoksteinetal.2011, author = {Ebenhoeh, Oliver and Houwaart, Torsten and Lokstein, Heiko and Schlede, Stephanie and Tirok, Katrin}, title = {A minimal mathematical model of nonphotochemical quenching of chlorophyll fluorescence}, series = {Biosystems : journal of biological and information processing sciences}, volume = {103}, journal = {Biosystems : journal of biological and information processing sciences}, number = {2}, publisher = {Elsevier}, address = {Oxford}, issn = {0303-2647}, doi = {10.1016/j.biosystems.2010.10.011}, pages = {196 -- 204}, year = {2011}, abstract = {Under natural conditions, plants are exposed to rapidly changing light intensities. To acclimate to such fluctuations, plants have evolved adaptive mechanisms that optimally exploit available light energy and simultaneously minimise damage of the photosynthetic apparatus through excess light. An important mechanism is the dissipation of excess excitation energy as heat which can be measured as nonphotochemical quenching of chlorophyll fluorescence (NPQ). In this paper, we present a highly simplified mathematical model that captures essential experimentally observed features of the short term adaptive quenching dynamics. We investigate the stationary and dynamic behaviour of the model and systematically analyse the dependence of characteristic system properties on key parameters such as rate constants and pool sizes. Comparing simulations with experimental data allows to derive conclusions about the validity of the simplifying assumptions and we further propose hypotheses regarding the role of the xanthophyll cycle in NPQ. We envisage that the presented theoretical description of the light reactions in conjunction with short term adaptive processes serves as a basis for the development of more detailed mechanistic models by which the molecular mechanisms of NPQ can be theoretically studied.}, language = {en} } @article{LoksteinHoextermannLeupoldetal.2009, author = {Lokstein, Heiko and Hoextermann, Ekkehard and Leupold, Dieter and Garab, Gyoezoe and Renger, Gernot}, title = {A tribute : Professor Dr. Paul Hoffmann (March 28, 1931-July 10, 2008), a scientist with a great collaborative spirit}, issn = {0166-8595}, doi = {10.1007/s11120-009-9414-6}, year = {2009}, language = {en} } @article{MikhailyukKnoxPaschenkoetal.2006, author = {Mikhailyuk, Igor K. and Knox, Peter P. and Paschenko, Vladimir Z. and Razjivin, Andrej P. and Lokstein, Heiko}, title = {Analysis of absorption spectra of purple bacterial reaction centers in the near infrared region by higher order derivative spectroscopy}, doi = {10.1016/j.bpc.2006.02.002}, year = {2006}, abstract = {Reaction centers (RCs) of purple bacteria are uniquely suited objects to study the mechanisms of the photosynthetic conversion of light energy into chemical energy. A recently introduced method of higher order derivative spectroscopy [I.K. Mikhailyuk, H. Lokstein, A.P. Razjivin, A method of spectral subband decomposition by simultaneous fitting the initial spectrum and a set of its derivatives, J. Biochem. Biophys. Methods 63 (2005) 10-23] was used to analyze the NIR absorption spectra of RC preparations from Rhodobacter (R.) sphaeroides strain 2R and Blastochloris (B.) viridis strain KH, containing bacteriochlorophyll (BChl) a and b, respectively. Q(y) bands of individual RC porphyrin components (BChls and bacteriopheophytins, BPheo) were identified. The results indicate that the upper exciton level Py+ of the photo-active BChl dimer in RCs of R. sphaeroides has an absorption maximum of 810nm. The blue shift of a complex integral band at approximately 800nm upon oxidation of the RC is caused primarily by bleaching of Py+, rather than by an electrochromic shift of the absorption band(s) of the monomeric BChls. Likewise, the disappearance of a band peaking at 842 nm upon oxidation of RCs from B. viridis indicates that this band has to be assigned to Py+, A blue shift of an absorption band at approximately 830nm upon oxidation of RCs of B. viridis is also essentially caused by the disappearance of Py+, rather than by an electrochromic shift of the absorption bands of monomeric BChls. Absorption maxima of the monomeric BCHls, B-B and B-A are at 802 and 797nm, respectively, in RCs of R. sphaeroides at room temperature. BPheo co-factors H-B and HA peak at 748 and 758 nm, respectively, at room temperature. For B. viridis RCs the spectral positions of HB and HA were found to be 796 and 816nm, respectively, at room temperature.}, language = {en} } @article{FritzLoksteinHackenbergetal.2007, author = {Fritz, Markus and Lokstein, Heiko and Hackenberg, Dieter and Welti, Ruth and Roth, Mary and Z{\"a}hringer, Ulrich and Fulda, Martin and Hellmeyer, Wiebke and Ott, Claudia and Wolter, Frank P. and Heinz, Ernst}, title = {Channeling of eukaryotic diacylglycerol into the biosynthesis of plastidial phosphatidylglycerol}, issn = {0021-9258}, doi = {10.1074/jbc.M606295200}, year = {2007}, abstract = {Plastidial glycolipids contain diacylglycerol (DAG) moieties, which are either synthesized in the plastids (prokaryotic lipids) or originate in the extraplastidial compartment (eukaryotic lipids) necessitating their transfer into plastids. In contrast, the only phospholipid in plastids, phosphatidylglycerol (PG), contains exclusively prokaryotic DAG backbones. PG contributes in several ways to the functions of chloroplasts, but it is not known to what extent its prokaryotic nature is required to fulfill these tasks. As a first step toward answering this question, we produced transgenic tobacco plants that contain eukaryotic PG in thylakoids. This was achieved by targeting a bacterial DAG kinase into chloroplasts in which the heterologous enzyme was also incorporated into the envelope fraction. From lipid analysis we conclude that the DAG kinase phosphorylated eukaryotic DAG forming phosphatidic acid, which was converted into PG. This resulted in PG with 2-3 times more eukaryotic than prokaryotic DAG backbones. In the newly formed PG the unique Delta 3-trans-double bond, normally confined to 3-transhexadecenoic acid, was also found in sn-2- bound cis-unsaturated C18 fatty acids. In addition, a lipidomics technique allowed the characterization of phosphatidic acid, which is assumed to be derived from eukaryotic DAG precursors in the chloroplasts of the transgenic plants. The differences in lipid composition had only minor effects on measured functions of the photosynthetic apparatus, whereas the most obvious phenotype was a significant reduction in growth.}, language = {en} } @misc{LoksteinKrikunovaTeuchneretal.2011, author = {Lokstein, Heiko and Krikunova, Maria and Teuchner, Klaus and Voigt, Bernd}, title = {Elucidation of structure-function relationships in photosynthetic light-harvesting antenna complexes by non-linear polarization spectroscopy in the frequency domain (NLPF)}, series = {Journal of plant physiology : biochemistry, physiology, molecular biology and biotechnology of plants}, volume = {168}, journal = {Journal of plant physiology : biochemistry, physiology, molecular biology and biotechnology of plants}, number = {12}, publisher = {Elsevier}, address = {Jena}, issn = {0176-1617}, doi = {10.1016/j.jplph.2010.12.012}, pages = {1488 -- 1496}, year = {2011}, abstract = {Photosynthetically active pigments are usually organized into pigment-protein complexes. These include light-harvesting antenna complexes (LHCs) and reaction centers. Site energies of the bound pigments are determined by interactions with their environment, i.e., by pigment-protein as well as pigment-pigment interactions. Thus, resolution of spectral substructures of the pigment-protein complexes may provide valuable insight into structure-function relationships. By means of conventional (linear) and time-resolved spectroscopic techniques, however, it is often difficult to resolve the spectral substructures of complex pigment-protein assemblies. Nonlinear polarization spectroscopy in the frequency domain (NLPF) is shown to be a valuable technique in this regard. Based on initial experimental work with purple bacterial antenna complexes as well as model systems NLPF has been extended to analyse the substructure(s) of very complex spectra, including analyses of interactions between chlorophylls and "optically dark" states of carotenoids in LHCs. The paper reviews previous work and outlines perspectives regarding the application of NLPF spectroscopy to disentangle structure-function relationships in pigment-protein complexes.}, language = {en} } @misc{LoksteinBetkeKrikunovaetal.2012, author = {Lokstein, Heiko and Betke, Alexander and Krikunova, Maria and Teuchner, Klaus and Voigt, Bernd}, title = {Elucidation of structure-function relationships in plant major light-harvesting complex (LHC II) by nonlinear spectroscopy}, series = {Photosynthesis research}, volume = {111}, journal = {Photosynthesis research}, number = {1-2}, publisher = {Springer}, address = {Dordrecht}, issn = {0166-8595}, doi = {10.1007/s11120-011-9700-y}, pages = {227 -- 235}, year = {2012}, abstract = {Conventional linear and time-resolved spectroscopic techniques are often not appropriate to elucidate specific pigment-pigment interactions in light-harvesting pigment-protein complexes (LHCs). Nonlinear (laser-) spectroscopic techniques, including nonlinear polarization spectroscopy in the frequency domain (NLPF) as well as step-wise (resonant) and simultaneous (non-resonant) two-photon excitation spectroscopies may be advantageous in this regard. Nonlinear spectroscopies have been used to elucidate substructure(s) of very complex spectra, including analyses of strong excitonic couplings between chlorophylls and of interactions between (bacterio) chlorophylls and "optically dark'' states of carotenoids in LHCs, including the major antenna complex of higher plants, LHC II. This article shortly reviews our previous study and outlines perspectives regarding the application of selected nonlinear laser-spectroscopic techniques to disentangle structure-function relationships in LHCs and other pigment-protein complexes.}, language = {en} } @article{NordhuesSchoettlerUngeretal.2012, author = {Nordhues, Andre and Sch{\"o}ttler, Mark Aurel and Unger, Ann-Katrin and Geimer, Stefan and Sch{\"o}nfelder, Stephanie and Schmollinger, Stefan and Ruetgers, Mark and Finazzi, Giovanni and Soppa, Barbara and Sommer, Frederik and M{\"u}hlhaus, Timo and Roach, Thomas and Krieger-Liszkay, Anja and Lokstein, Heiko and Luis Crespo, Jose and Schroda, Michael}, title = {Evidence for a role of VIPP1 in the structural organization of the photosynthetic apparatus in chlamydomonas}, series = {The plant cell}, volume = {24}, journal = {The plant cell}, number = {2}, publisher = {American Society of Plant Physiologists}, address = {Rockville}, issn = {1040-4651}, doi = {10.1105/tpc.111.092692}, pages = {637 -- 659}, year = {2012}, abstract = {The vesicle-inducing protein in plastids (VIPP1) was suggested to play a role in thylakoid membrane formation via membrane vesicles. As this functional assignment is under debate, we investigated the function of VIPP1 in Chlamydomonas reinhardtii. Using immunofluorescence, we localized VIPP1 to distinct spots within the chloroplast. In VIPP1-RNA interference/artificial microRNA cells, we consistently observed aberrant, prolamellar body-like structures at the origin of multiple thylakoid membrane layers, which appear to coincide with the immunofluorescent VIPP1 spots and suggest a defect in thylakoid membrane biogenesis. Accordingly, using quantitative shotgun proteomics, we found that unstressed vipp1 mutant cells accumulate 14 to 20\% less photosystems, cytochrome b(6)f complex, and ATP synthase but 30\% more light-harvesting complex II than control cells, while complex assembly, thylakoid membrane ultrastructure, and bulk lipid composition appeared unaltered. Photosystems in vipp1 mutants are sensitive to high light, which coincides with a lowered midpoint potential of the Q(A)/Q(A)(-) redox couple and increased thermosensitivity of photosystem II (PSII), suggesting structural defects in PSII. Moreover, swollen thylakoids, despite reduced membrane energization, in vipp1 mutants grown on ammonium suggest defects in the supermolecular organization of thylakoid membrane complexes. Overall, our data suggest a role of VIPP1 in the biogenesis/assembly of thylakoid membrane core complexes, most likely by supplying structural lipids.}, language = {en} } @article{LeupoldLoksteinScheer2006, author = {Leupold, Dieter and Lokstein, Heiko and Scheer, Hugo}, title = {Excitation energy transfer between (bacterio)chlorophylls : the role of excitonic coupling}, year = {2006}, language = {en} }