Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Chlorophyll”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 991 records · Page 55Linked to original sources
PubMed2004

Facile synthesis of chlorophyll analog possessing a disulfide bond and formation of self-assembled monolayer on gold surface.

A chlorophyll analog forming self-assembled monolayers (SAMs) on a gold surface was synthesized for the first time. 13(2)-(Demethoxycarbonyl)pheophorbide-a, which was converted from naturally occurring chlorophyll-a, was condensed with 2-hydroxyethyl disulfide to give a chlorin dyad linked by a disulfide bond. The chlorin analog was spontaneously immobilized on a gold substrate by soaking in an acetone solution of the dyad for 24 h. The resulting gold plate exhibited a visible absorption spectrum with about 420- and 675-nm maxima as the Soret and Qy peaks, respectively, indicating that chlorin pi-conjugates were modified on the gold substrate through Au-S bonding. Both visible absorption and fluorescence emission bands of the chlorin chromophores on the gold substrate were red-shifted compared with those of the synthesized chlorin dyad in a homogeneous acetone solution. The measured absorbance at the Soret maximum suggests that the chlorin chromophores on the gold plate were densely packed on a gold surface to form a SAM. Cathodic photocurrents were generated from SAMs of the chlorins on a gold substrate with irradiation of visible-lights above 400 nm. Photoinduced electron transfer from chlorins on the gold substrate to oxygen molecules in an electrolyte solution were attributed to the cathodic photocurrent generation.

Chlorophyll↗
PubMed2005

Plastid structure and chlorophyll content in leaf primordia of onion bulbs.

Angiosperms do not synthesize chlorophyll in the dark. Here we show that leaf primordia in onion bulbs are green, though they developing in dark conditions. We present results that show plastids in green primordia are chloroplasts, and that they contain chlorophyll as well as embryos in seeds of certain angiosperms.

Chlorophyll↗
PubMed2006

Chlorophyll metabolism.

Since the 1970s, researchers have proposed several regulatory pathways governing chlorophyll metabolism, but only recently have the underlying molecular mechanisms been elucidated. The recent data indicate that such regulatory systems are more complex than originally anticipated. For instance, the pathways involve a series of protein-protein interactions, including complex formation, the dual localization of enzymes within chloroplasts, and a novel protein degradation mechanism that is triggered by pigments. Furthermore, several lines of evidence suggest that chlorophyll metabolism might not only significantly impact the assembly of photosynthetic machineries but also influence processes such as programmed cell death, the 'stay-green' phenomenon, and chloroplast-nucleus communication.

Chlorophyll↗
PubMed2001

Isolation of membrane protein subunits in their native state: evidence for selective binding of chlorophyll and carotenoid to the b(6) subunit of the cytochrome b(6)f complex.

Cytochrome (cyt) b-c complexes play a central role in electron transfer chains and are almost ubiquitous in nature. Although similar in their basic structure and function, the cyt b(6)f complex of photosynthetic membranes and its counterpart, the mitochondrial cyt bc(1) complex, show some characteristic differences which cannot be explained by the high resolution structure of the cyt bc(1) complex alone. Especially the presence of a chlorophyll molecule is a striking feature of all cyt b(6)f complex preparations described so far, imposing questions as to its structural and functional role. To allow a more detailed characterization, we here report the preparation of native subunits cyt b(6) and IV starting from a monomeric cyanobacterial cyt b(6)f complex. Spectroscopical and reversed-phase HPLC analyses of the purified cyt b(6) subunit showed that it contained not only two b-type hemes, but also one chlorophyll a molecule and a cyanobacterial carotenoid, echinenone. Evidence for selective binding of both pigments to this subunit is presented and their putative function is discussed.

Carotenoids↗
PubMed2002

Valinomycin sensitivity proves that light-induced thylakoid voltages result in millisecond phase of chlorophyll fluorescence transients.

Upon sudden exposure of plants to an actinic light of saturating intensity, the yield of chlorophyll fluorescence increases typically by 200-400% of the initial O-level. At least three distinct phases of these O-J-I-P transients can be resolved: O-J (0.05-5 ms), J-I (5-50 ms), and I-P (50-1000 ms). In thylakoid membranes, the J-I increase accounts for approximately 30% of the total fluorescence increase; in Photosystem II membranes, the J-I phase is always lacking. In the presence of the ionophore valinomycin, which is known to inhibit specifically the formation of membrane voltages, the magnitude of the J-I phase is clearly diminished; in the presence of valinomycin supplemented by potassium, the J-I phase is fully suppressed. We conclude that the light-driven formation of the thylakoid-membrane voltage results in an increase of the chlorophyll excited-state lifetime, a phenomenon explainable by the electric-field-induced shift of the free-energy level of the primary radical pair [Dau and Sauer, Biochim. Biophys. Acta 1102 (1992) 91]. The assignment of the J-I increase in the fluorescence yield enhances the potential of using O-J-I-P fluorescence transients for investigations on photosynthesis in intact organisms. A putative role of thylakoid voltages in protection of PSII against photoinhibitory damage is discussed.

Anti-Bacterial Agents↗
PubMed1999

Molecular structure, localization and function of biliproteins in the chlorophyll a/d containing oxygenic photosynthetic prokaryote Acaryochloris marina.

We investigated the localization, structure and function of the biliproteins of the oxygenic photosynthetic prokaryote Acaryochloris marina, the sole organism known to date that contains chlorophyll d as the predominant photosynthetic pigment. The biliproteins were isolated by means of sucrose gradient centrifugation, ion exchange and gel filtration chromatography. Up to six biliprotein subunits in a molecular mass range of 15.5-18.4 kDa were found that cross-reacted with antibodies raised against phycocyanin or allophycocyanin from a red alga. N-Terminal sequences of the alpha- and beta-subunits of phycocyanin showed high homogeneity to those of cyanobacteria and red algae, but not to those of cryptomonads. As shown by electron microscopy, the native biliprotein aggregates are organized as rod-shaped structures and located on the cytoplasmic side of the thylakoid membranes predominantly in unstacked thylakoid regions. Biochemical and spectroscopic analysis revealed that they consist of four hexameric units, some of which are composed of phycocyanin alone, others of phycocyanin together with allophycocyanin. Spectroscopic analysis of isolated photosynthetic reaction center complexes demonstrated that the biliproteins are physically attached to the photosystem II complexes, transferring light energy to the photosystem II reaction center chlorophyll d with high efficiency.

Amino Acid Sequence↗
PubMed2000

Förster excitation energy transfer in peridinin-chlorophyll-a-protein.

Time-resolved fluorescence anisotropy spectroscopy has been used to study the chlorophyll a (Chl a) to Chl a excitation energy transfer in the water-soluble peridinin-chlorophyll a-protein (PCP) of the dinoflagellate Amphidinium carterae. Monomeric PCP binds eight peridinins and two Chl a. The trimeric structure of PCP, resolved at 2 A (, Science. 272:1788-1791), allows accurate calculations of energy transfer times by use of the Förster equation. The anisotropy decay time constants of 6.8 +/- 0.8 ps (tau(1)) and 350 +/- 15 ps (tau(2)) are respectively assigned to intra- and intermonomeric excitation equilibration times. Using the ratio tau(1)/tau(2) and the amplitude of the anisotropy, the best fit of the experimental data is achieved when the Q(y) transition dipole moment is rotated by 2-7 degrees with respect to the y axis in the plane of the Chl a molecule. In contrast to the conclusion of, Biochemistry. 23:1564-1571) that the refractive index (n) in the Förster equation should be equal to that of the solvent, n can be estimated to be 1.6 +/- 0.1, which is larger than that of the solvent (water). Based on our observations we predict that the relatively slow intermonomeric energy transfer in vivo is overruled by faster energy transfer from a PCP monomer to, e.g., the light-harvesting a/c complex.

Carotenoids↗
PubMed2004

Electrochromic shift of chlorophyll absorption in photosystem I from Synechocystis sp. PCC 6803: a probe of optical and dielectric properties around the secondary electron acceptor.

Nanosecond absorption dynamics at approximately 685 nm after excitation of photosystem I (PS I) from Synechocystis sp. PCC 6803 is consistent with electrochromic shift of absorption bands of the Chl a pigments in the vicinity of the secondary electron acceptor A(1). Based on experimental optical data and structure-based simulations, the effective local dielectric constant has been estimated to be between 3 and 20, which suggests that electron transfer in PS I is accompanied by considerable protein relaxation. Similar effective dielectric constant values have been previously observed for the bacterial photosynthetic reaction center and indicate that protein reorganization leading to effective charge screening may be a necessary structural property of proteins that facilitate the charge transfer function. The data presented here also argue against attributing redmost absorption in PS I to closely spaced antenna chlorophylls (Chls) A38 and A39, and suggest that optical transitions of these Chls, along with that of connecting chlorophyll (A40) lie in the range 680-695 nm.

Chlorophyll↗
PubMed1965

Fluorescence decay studies of chlorophyll A in vivo.

The study of the fluorescence of chlorophyll a offers a useful approach toward better understanding of the primary act of photosynthesis. This paper describes new measurements of the decay of chlorophyll a fluorescence in vivo, made with a considerably improved oscilloscopic-display technique. The main result is the identification of two decay periods both of the order of a few nanoseconds. Possible interpretations of this phenomenon are discussed.

Chlorophyll↗
PubMed1966

Spectral studies of a chlorophyll pigment with fluorescence maximum at 698 mu.

A chlorophyll type pigment (F698) fluorescing maximally at 698 mmu at 77 degrees K has been observed in preparations of chlorophyll. This fluorescence is quenched by small amounts of naturally occurring materials, including plastoquinone and the ubiquinones, and by nitrobenzene, probably by formation of a nonfluorescent complex. Fluorescence quenching does not occur in the presence of carotenes, xanthophylls, or reduced plastoquinone and ubiquinone. The fluorescence is sharply temperature dependent, with a steep rise in intensity occurring at 165 degrees K. At 77 degrees K the fluorescence yield is between 0.8 and 1.0. The red absorption maximum of the pigment is at 675 mmu at room temperature and at 688 mmu at 77 degrees K. In vivo, a low temperature emission is also observed at 698 mmu, and this fluorescence is quenched by nitrobenzene. It is proposed that the pigment found in vitro is also the one responsible for emission at 698 mmu in vivo. A reaction of F698 with plastoquinone is suggested as the primary photochemical step in system II of photosynthesis.

Chlorophyll↗
PubMed1968

Light-induced changes in the fluorescence yield of chlorophyll a in vivo. I. Anacystis nidulans.

he fluorescence yield of chlorophyll a in dark adapted Anacystis nidulans undergoes a slow change with continuous illumination. After the completion of the initial fast transient, the fluorescence yield rises from the level S to a plateau M within a minute, declining only after prolonged illumination. Both normal and 1,1-dimethyl-3(3'4'-dichloro)-phenylurea (DCMU)-poisoned Anacystis are capable of these changes. In normal Anacystis, the slow increase in the fluorescence yield (S --> M) requires light absorbed in system II while light absorbed in system I is ineffective. In DCMU-poisoned Anacystis, however, these changes are also promoted by light absorbed in system I. Addition of carbonyl cyanide p-trifluoromethoxy phenylhydrazone (FCCP), a photophosphorylation uncoupler acting near the photosynthetic electron transport chain, abolishes the rise from S to M in normal but has no effect in the DCMU-poisoned system. Phlorizin, a phosphorylase inhibitor, has very little effect. These results suggest that the light-induced variation in the fluorescence yield is related to the conformational changes which accompany photophosphorylation. The fluorescence yield of the auxiliary pigment phycocyanin remains constant throughout the interval of the light-induced changes in the fluorescence yield of chlorophyll a. Consequently, the fluorescence spectrum of the alga is variable on continuous illumination.

Antimetabolites↗
PubMed1968

Low temperature absorption spectra of chlorophyll a in polar and nonpolar solvents.

Absorption spectra of chlorophyll a were measured in polar and non-polar solvents, as a function of temperature from 298 degrees to 77 degrees K. Both dilute and concentrated solutions were examined. In both types of solvents at room temperature, the absorption spectra of concentrated solutions differ from dilute ones in that the half width of the main red absorption band is greater, and all bands are shifted to longer wavelengths. These differences are largely due to the presence of dimers when the pigment concentration is high. In dilute ethanol solutions, where the chlorophyll is unassociated, cooling causes a red shift in all bands which is due to the increased polarity of the solvent at low temperature. On cooling at high concentrations in ethanol and EPA, a new band appears near 700 nm. This band is attributed to dimers present prior to cooling, but absorbing at shorter wavelengths at room temperature. In nonpolar solvents, a band near 700 nm appears at the solvent freezing point. In these solvents, the "700" nm absorption is attributed to dimers, and/or small polymers, partly formed by cooling. A change in aggregate geometry when the solvent becomes viscous or frozen can account for the appearance of this "700" nm absorption band at low temperature, in polar and nonpolar media.

Chlorophyll↗
PubMed1981

Lifetime of fluorescence from light-harvesting chlorophyll a/b proteins. Excitation intensity dependence.

The fluorescence from a purified, aggregate form of the light-harvesting chlorophyll a/b protein has a lifetime of 1.2 +/- 0.5 ns at low excitation intensity, but the lifetime decreases significantly when the intensity of the 20-ps, 530-nm excitation pulse is increased above about 10(16) photons/cm2. A solubilized, monomeric form of the protein, on the other hand, has a fluorescence lifetime of 3.1 +/- 0.3 ns independent of excitation intensity from 10(14)-10(18) photons/cm2/pulse. We interpret the lifetime shortening in the aggregates and the lack of shortening in monomers in terms of exciton annihilation, facilitated in the aggregate by the larger population of interacting chlorophylls.

Chlorophyll↗
PubMed1982

Formation of crystalline arrays of chlorophyll a/b - light-harvesting protein by membrane reconstitution.

The structure of the major protein constituent of photosynthetic membranes in higher plants, the chlorophyll a/b-light harvesting complex (LHC), was studied by x-ray diffraction and electron microscopy. The LHC was purified from Triton X-100 solubilized thylakoid membranes of the pea, and contained 6 mol of chlorophylls a and b per mole of a polypeptide of 27,000 molecular weight. X-ray diffraction showed that in the presence of 10 mM MgCl2, purified LHC forms planar aggregates that stack with a period of 51 A. Within each layer, LHC molecules pack with a center-to-center distance of 85 A but without long-range order. However, when LHC is incorporated into single-walled vesicles of plant lecithin, the addition of NaCl above 10 mM, or MgCl2 above 2 mM, led to the formation of plaques of hexagonal lattices, with a lattice constant of 125 A. The large domain size and high degree of order in the plane of the membrane are evident from the sharp lattice lines observed to 7 A resolution on the equator of the x-ray pattern. Freeze-fracture electron micrographs demonstrated an aligned stacking of the lattices in adjacent membranes, resulting in crystallinity in the third dimension over short distances. Micrographs of negatively stained membranes revealed a hexagonal lattice of the same lattice constant, formed by surface-exposed parts of the LHC molecules which are probably responsible for the ordered stacking of lattices. In both the LHC aggregates and in the reconstituted membrane lattices the diffracted x-ray intensities at 10-A spacing on the equator indicate that the LHC molecule contains paralled alpha-helices or beta-sheets that are oriented perpendicular to the planar arrays.

Chlorophyll↗
PubMed1994

Excited state dynamics in chlorophyll-based antennae: the role of transfer equilibrium.

We present computer simulations of excited state dynamics in models of PS I and PS II which are based upon known structural and spectral properties of the antennae. In particular, these models constrain the pigment binding sites to three-dimensional volumes determined from molecular properties of the antenna complexes. The simulations demonstrate that within a 10-30 ps after light absorption, rapid energy transfer among coupled antenna chlorophylls leads to a quasiequilibrium state in which the fraction of the excited state on any antenna chlorophyll, normalized to the total excited state remaining on the model, remains constant with time. We describe this quasiequilibrium state as a "transfer equilibrium" (TE) state because of its dependence on the rates of processes that couple excited state motion and quenching in the antenna as well as on the individual antenna site energies and temperature. The TE state is not a true equilibrium in that loss of the excited state primarily due to photochemistry (but also due to fluorescence, thermal emission, and intersystem crossing) continues once TE is established. Depending on the dynamics of the system, the normalized distribution of excited state at TE may differ substantially from the Boltzmann distribution (the state of the model at infinite time in the absence of any avenues for decay of excited state). The models predict lifetimes, equilibration times, and photochemical yields that are in agreement with experimental data and affirm trap-limited dynamics in both photosystems. The rapid occurrence of TE states implies that any excited state dynamics that depends on antenna structure and excitation wavelength must occur before the TE state is established. We demonstrate that the excited state distribution of the TE state is central to determining the excited state lifetime and quantum efficiency of photochemistry.

Binding Sites↗
PubMed1999

Electronic spectra of PS I mutants: the peripheral subunits do not bind red chlorophylls in Synechocystis sp. PCC 6803.

Steady-state fluorescence and absorption spectra have been obtained in the Qy spectral region (690-780 nm and 600-750 nm, respectively) for several subunit-deficient photosystem I mutants from the cyanobacterium Synechocystis sp. PCC 6803. The 77 K fluorescence spectra of the wild-type and subunit-deficient mutant photosystem I particles are all very similar, peaking at approximately 720 nm with essentially the same excitation spectrum. Because emission from far-red chlorophylls absorbing near 708 nm dominates low-temperature fluorescence in Synechocystis sp., these pigments are not coordinated to any the subunits PsaF, Psa I, PsaJ, PsaK, PsaL, or psaM. The room temperature (wild-type-mutant) absorption difference spectra for trimeric mutants lacking the PsaF/J, PsaK, and PsaM subunits suggest that these mutants are deficient in core antenna chlorophylls (Chls) absorbing near 685, 670, 675, and 700 nm, respectively. The absorption difference spectrum for the PsaF/J/I/L-deficient photosystem I complexes at 5 K reveals considerably more structure than the room-temperature spectrum. The integrated absorbance difference spectra (when normalized to the total PS I Qy spectral area) are comparable to the fractions of Chls bound by the respective (groups of) subunits, according to the 4-A density map of PS I from Synechococcus elongatus. The spectrum of the monomeric PsaL-deficient mutant suggests that this subunit may bind pigments absorbing near 700 nm.

Chlorophyll↗
PubMed2000

Chlorophyll fluorescence quenching in isolated light harvesting complexes induced by zeaxanthin.

Non-photochemical quenching of chlorophyll fluorescence in plants occurs in the light harvesting antenna of photosystem II and is regulated by the xanthophyll cycle. A new in vitro model for this process has been developed. Purified light harvesting complexes above the detergent critical micelle concentration have a stable high fluorescence yield but a rapidly inducible fluorescence quenching occurs upon addition of zeaxanthin. Violaxanthin was without effect, lutein and antheraxanthin induced a marginal response, whereas the violaxanthin analogue, auroxanthin, induced strong quenching. Quenching was not caused by aggregation of the complexes but was accompanied by a spectral broadening and red shift, indicating a zeaxanthin-dependent alteration in the chlorophyll environment.

Chlorophyll↗