spheroidene and neurosporene

spheroidene has been researched along with neurosporene* in 7 studies

Other Studies

7 other study(ies) available for spheroidene and neurosporene

ArticleYear
Effect of Illumination Intensity and Inhibition of Carotenoid Biosynthesis on Assembly of Peripheral Light-Gathering Complexes in Purple Sulfur Bacteria C Allochromatium vinosum ATCC 17899.
    Mikrobiologiia, 2016, Volume: 85, Issue:4

    Effect of illumination intensity and inhibition of carotenoid biosynthesis on assemblage of different spectral types of LH2 complexes in a purple sulfur bacterium Allochromatium (Alc.) vinosum ATCC 17899 was studied. Under illumination of 1200 and 500 lx, the complexes B800-850 and B800-840 and B800-820 were assembled. While rhodopine was the major carotenoid in all spectral types of the LH2 complex, a certain- increase in the content of carotenoids with higher numbers of conjugated double bonds (anhydrorhodovibrin and didehydrorhodovibrin) was observed in the B800-820 complex. At 1200 lx, the cells grew slowly at diphe- nylamine (DPA) concentrations not exceeding 53 .iM, while at illumination intensity decreased to 500 Ix they could grow at 71 jiM DPA (DPA cells). Independent on illumination level, the inhibitor is supposed to impair the functioning of phytoine synthetase (resulting in a decrease in the total carotenoid content) and of phyto- ine desturase, which results in formation of neurosporene hydroxy derivatives and ;-carotene. In the cells grown at 500 lx, small amounts of spheroidene and.OH-spheroidene were detected. These carotenoids were originally found under conditions of carotenoid synthesis inhibition in bacteria with spirilloxanthin as the major carotenoid. Carotenoid content in the LH2 complexes isolated from the DPA cells was -15% of the control (without inhibition) for the B800-850 and -20%of the control for the B800-820 and B800-840 DPA complexes. Compared to the DPA pigment-containing membranes, the DPA complexes were enriched with -carotenoids due to- disintegration of some carotenoid-free complexes in the course of isolation. These results support the supposition that some of the B800-820, B800-840, and B800-850 complexes may be Assembled in the cells of Alc. vinosum ATCC 17899 without carotenoids. Comparison of the characteristics obtained for Alc. vinosum ATCC 17899 and the literature data on strain D of the same bacteria shows that they belong to two different strains, rather than to one as was previously supposed.

    Topics: Bacterial Proteins; Carotenoids; Chromatiaceae; Culture Media; Diphenylamine; Dose-Response Relationship, Radiation; Gene Expression; Ligases; Light; Light-Harvesting Protein Complexes; Mixed Function Oxygenases; Xanthophylls; zeta Carotene

2016
Carotenogenesis gene cluster and phytoene desaturase catalyzing both three- and four-step desaturations from Rhodobacter azotoformans.
    FEMS microbiology letters, 2012, Volume: 333, Issue:2

    A carotenogenesis gene cluster from the purple nonsulfur photosynthetic bacterium Rhodobacter azotoformans CGMCC 6086 was cloned. A total of eight carotenogenesis genes ( crtA , crtI , crtB , tspO , crtC , crtD , crtE , and crtF ) were located in two separate regions within the genome, a 4.9 kb region containing four clustered genes of crtAIB - tspO and a 5.3 kb region containing four clustered genes of crtCDEF . The organization was unusual for a carotenogenesis gene cluster in purple photosynthetic bacteria. A gene encoding phytoene desaturase ( CrtI ) from Rba. azotoformans was expressed in Escherichia coli. The recombinant CrtI could catalyze both three- and four-step desaturations of phytoene to produce neurosporene and lycopene, and the relative contents of neurosporene and lycopene formed by CrtI were approximately 23% and 75%, respectively. Even small amounts of five-step desaturated 3,4-didehydrolycopene could be produced by CrtI . This product pattern was novel because CrtI produced only neurosporene leading to spheroidene pathway in the cells of Rba. azotoformans. In the in vitro reaction, the relative content of lycopene in desaturated products increased from 19.6% to 62.5% when phytoene reduced from 2.6 to 0.13 μM. The results revealed that the product pattern of CrtI might be affected by the kinetics.

    Topics: Bacterial Proteins; Carotenoids; Cloning, Molecular; Electrophoresis, Polyacrylamide Gel; Enzyme Activation; Escherichia coli; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Genes, Bacterial; Genetic Vectors; Lycopene; Multigene Family; Oxidoreductases; Recombinant Proteins; Rhodobacter

2012
Carotenoid radical formation: dependence on conjugation length.
    The journal of physical chemistry. B, 2011, Aug-04, Volume: 115, Issue:30

    The relative energy of carotenoid neutral radicals formed by proton loss from the radical cations of linear carotenoids has been examined as a function of conjugation length from n = 15 to 9. For a maximum conjugation length of n = 15 (bisdehydrolycopene, a symmetrical compound), proton loss can occur from any of the 10 methyl groups, with proton loss from the methyl group at position C1 or C1' being the most favorable. In contrast, the most energetically favorable proton loss from the radical cations of lycopene, neurosporene, spheroidene, spheroidenone, spirilloxanthin, and anhydrorhodovibrin occurs from methylene groups that extend from the conjugated system. For example, decreasing the conjugation length to n = 11 (lycopene) by saturation of the double bonds C3-C4 and at C3'-C4' of bisdehydrolycopene favors proton loss at C4 or C4' methylene groups. Saturation at C7'-C8' in the case of neurosporene, spheroidene, and spheroidenone (n = 9, 10, 11) favors the formation of a neutral radical at the C8' methylene group. Saturation of C1-C2 by addition of a methoxy group to a bisdehydrolycopene-like structure with conjugation of n = 12 or 13 (anhydrorhodovibrin, spirilloxanthin) favors proton loss at the C2 methylene group. As a consequence of deprotonation of the radical cation, the unpaired electron spin distribution changes so that larger β-methyl proton couplings occur for the neutral radicals (13-16 MHz) than for the radical cation (7-10 MHz), providing a means to identify possible carotenoid radicals in biological systems by Mims ENDOR.

    Topics: Carotenoids; Electron Spin Resonance Spectroscopy; Free Radicals; Lycopene; Protons; Thermodynamics; Xanthophylls

2011
Ultrafast time-resolved carotenoid to-bacteriochlorophyll energy transfer in LH2 complexes from photosynthetic bacteria.
    The journal of physical chemistry. B, 2008, Aug-28, Volume: 112, Issue:34

    Steady-state and ultrafast time-resolved optical spectroscopic investigations have been carried out at 293 and 10 K on LH2 pigment-protein complexes isolated from three different strains of photosynthetic bacteria: Rhodobacter (Rb.) sphaeroides G1C, Rb. sphaeroides 2.4.1 (anaerobically and aerobically grown), and Rps. acidophila 10050. The LH2 complexes obtained from these strains contain the carotenoids, neurosporene, spheroidene, spheroidenone, and rhodopin glucoside, respectively. These molecules have a systematically increasing number of pi-electron conjugated carbon-carbon double bonds. Steady-state absorption and fluorescence excitation experiments have revealed that the total efficiency of energy transfer from the carotenoids to bacteriochlorophyll is independent of temperature and nearly constant at approximately 90% for the LH2 complexes containing neurosporene, spheroidene, spheroidenone, but drops to approximately 53% for the complex containing rhodopin glucoside. Ultrafast transient absorption spectra in the near-infrared (NIR) region of the purified carotenoids in solution have revealed the energies of the S1 (2(1)Ag-)-->S2 (1(1)Bu+) excited-state transitions which, when subtracted from the energies of the S0 (1(1)Ag-)-->S2 (1(1)Bu+) transitions determined by steady-state absorption measurements, give precise values for the positions of the S1 (2(1)Ag-) states of the carotenoids. Global fitting of the ultrafast spectral and temporal data sets have revealed the dynamics of the pathways of de-excitation of the carotenoid excited states. The pathways include energy transfer to bacteriochlorophyll, population of the so-called S* state of the carotenoids, and formation of carotenoid radical cations (Car*+). The investigation has found that excitation energy transfer to bacteriochlorophyll is partitioned through the S1 (1(1)Ag-), S2 (1(1)Bu+), and S* states of the different carotenoids to varying degrees. This is understood through a consideration of the energies of the states and the spectral profiles of the molecules. A significant finding is that, due to the low S1 (2(1)Ag-) energy of rhodopin glucoside, energy transfer from this state to the bacteriochlorophylls is significantly less probable compared to the other complexes. This work resolves a long-standing question regarding the cause of the precipitous drop in energy transfer efficiency when the extent of pi-electron conjugation of the carotenoid is extended from ten to eleven conjugated ca

    Topics: Algorithms; Bacterial Proteins; Bacteriochlorophylls; Carotenoids; Cold Temperature; Energy Transfer; Kinetics; Light-Harvesting Protein Complexes; Models, Molecular; Rhodobacter sphaeroides; Rhodopseudomonas; Spectrometry, Fluorescence; Spectrophotometry; Spectroscopy, Near-Infrared; Temperature; Time Factors

2008
Ultrafast dynamics and excited state spectra of open-chain carotenoids at room and low temperatures.
    The journal of physical chemistry. B, 2007, May-31, Volume: 111, Issue:21

    Many of the spectroscopic features and photophysical properties of carotenoids are explained using a three-state model in which the strong visible absorption of the molecules is associated with an S0 (1(1)Ag-) --> S2 (1(1)Bu+) transition, and the lowest lying singlet state, S1 (2(1)Ag-), is a state into which absorption from the ground state is forbidden by symmetry. However, semiempirical and ab initio quantum calculations have suggested additional excited singlet states may lie either between or in the vicinity of S1 (2(1)Ag-) and S2 (1(1)Bu+), and some ultrafast spectroscopic studies have reported evidence for these states. One such state, denoted S*, has been implicated as an intermediate in the depopulation of S2 (1(1)Bu+) and as a pathway for the formation of carotenoid triplet states in light-harvesting complexes. In this work, we present the results of an ultrafast, time-resolved spectroscopic investigation of a series of open-chain carotenoids derived from photosynthetic bacteria and systematically increasing in their number of pi-electron carbon-carbon double bonds (n). The molecules are neurosporene (n = 9), spheroidene (n = 10), rhodopin glucoside (n = 11), rhodovibrin (n = 12), and spirilloxanthin (n = 13). The molecules were studied in acetone and CS2 solvents at room temperature. These experiments explore the effect of solvent polarity and polarizability on the spectroscopic and kinetic behavior of the molecules. The molecules were also studied in ether/isopentane/ethanol (EPA) glasses at 77 K, in which the spectral resolution is greatly enhanced. Analysis of the data using global fitting techniques has revealed the ultrafast dynamics of the excited states and spectral changes associated with their decay, including spectroscopic features not previously reported. The data are consistent with S* being identified with a twisted conformational structure, the yield of which is increased in molecules having longer pi-electron conjugations. In particular, for the longest molecule in the series, spirilloxanthin, the experiments and a detailed quantum computational analysis reveal the presence of two S* states associated with relaxed S1 (2(1)Ag-) conformations involving nearly planar 6-s-cis and 6-s-trans geometries. We propose that in polar solvents, the ground state of spirilloxanthin takes on a corkscrew conformation that generates a net solute dipole moment while decreasing the cavity formation energy. Upon excitation and relaxation into the S1

    Topics: Carotenoids; Glucosides; Kinetics; Models, Chemical; Molecular Structure; Quantum Theory; Rhodobacter sphaeroides; Rhodopseudomonas; Sensitivity and Specificity; Spectrum Analysis; Temperature; Vibration; Xanthophylls

2007
Carotenoid radical cation formation in LH2 of purple bacteria: a quantum chemical study.
    The journal of physical chemistry. B, 2006, Nov-30, Volume: 110, Issue:47

    In LH2 complexes of Rhodobacter sphaeroides the formation of a carotenoid radical cation has recently been observed upon photoexcitation of the carotenoid S2 state. To shed more light onto the yet unknown molecular mechanism leading to carotenoid radical formation in LH2, the interactions between carotenoid and bacteriochlorophyll in LH2 are investigated by means of quantum chemical calculations for three different carotenoids--neurosporene, spheroidene, and spheroidenone--using time-dependent density functional theory. Crossings of the calculated potential energy curve of the electron transfer state with the bacteriochlorophyll Qx state and the carotenoid S1 and S2 states occur along an intermolecular distance coordinate for neurosporene and spheroidene, but for spheroidenone no crossing of the electron transfer state with the carotenoid S1 state could be found. By comparison with recent experiments where no formation of a spheroidenone radical cation has been observed, a molecular mechanism for carotenoid radical cation formation is proposed in which it is formed via a vibrationally excited carotenoid S1 or S*state. Arguments are given why the formation of the carotenoid radical cation does not proceed via the Qx, S2, or higher excited electron transfer states.

    Topics: Algorithms; Bacterial Proteins; Bacteriochlorophylls; Carotenoids; Cations; Electron Transport; Energy Transfer; Free Radicals; Light; Light-Harvesting Protein Complexes; Protein Conformation; Proteobacteria; Quantum Theory; Rhodobacter sphaeroides; Time Factors

2006
Photo-oxidative stress in Rhodobacter sphaeroides: protective role of carotenoids and expression of selected genes.
    Microbiology (Reading, England), 2005, Volume: 151, Issue:Pt 6

    In Rhodobacter sphaeroides, carotenoids are essential constituents of the photosynthetic apparatus and are assumed to prevent the formation of singlet oxygen by quenching of triplet bacteriochlorophyll a (BChl a) in vivo. It was shown that small amounts of singlet oxygen are generated in vivo by incubation of R. sphaeroides under high light conditions. However, growth and survival rates were not affected. Higher amounts of singlet oxygen were generated by BChl a in a carotenoid-deficient strain and led to a decrease in growth and survival rates. The data support earlier results on the pivotal role of carotenoids in the defence against stress caused by singlet oxygen. Results obtained under photo-oxidative stress conditions with strains impaired in carotenoid synthesis suggest that sphaeroidene and neurosporene provide less protection against methylene-blue-generated singlet oxygen than sphaeroidenone in vivo. Despite their protective function against singlet oxygen, relative amounts of carotenoids did not accumulate in R. sphaeroides wild-type cultures under photo-oxidative stress, and relative mRNA levels of phytoene dehydrogenase and sphaeroidene monooxygenase did not increase. In contrast, singlet oxygen specifically induced the expression of glutathione peroxidase and a putative Zn-dependent hydrolase, but mRNA levels of hydrogen-peroxide-degrading catalase E were not significantly affected by photo-oxidative stress. Based on these results, it is suggested that singlet oxygen acts as a specific signal for gene expression in R. sphaeroides. Presumably transcriptional regulators exist to specifically induce the expression of genes involved in the response to stress caused by singlet oxygen.

    Topics: Adaptation, Physiological; Carotenoids; Catalase; Gene Expression Regulation, Bacterial; Glutathione Peroxidase; Hydrolases; Oxidative Stress; Oxidoreductases; Reverse Transcriptase Polymerase Chain Reaction; Rhodobacter sphaeroides; RNA, Bacterial; RNA, Messenger; Singlet Oxygen; Transcription, Genetic

2005