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1.
M Lutz I Agalidis G Hervo R J Cogdell F Reiss-Husson 《Biochimica et biophysica acta》1978,503(2):287-303
The carotenoids bound to reaction centers of wild, Ga and GIC strains of Rhodopseudomonas spheroides, of Rhodospirrillum rubrum, strain S1 and of Rhodopseudomonas viridis, yield very similar, but unusual resonance Raman spectra. Through a comparison with resonance Raman spectra of 15,15'-cis-beta-carotene, these carotenoids are shown to assume cis conformations, while the corresponding chromatophores contain all-trans forms only. These cis conformations likely are identical for all the carotenoids studied. They remain unaffected by variations of temperature from 20 to 300 K as well as by the redox state of P-870. They are unstable, being rapidly isomerised towards the all-trans forms when extracted from the reaction centers. The possible nature of these conformers is discussed on the basis of their electronic and vibrational spectra. 相似文献
2.
We report and discuss Raman spectra of bacteriochlorophyll and of bacteriopheophytin obtained by resonance effect in their QX and Soret electronic bands. Selective excitation of spectra of either of these molecules in reaction centers of , strains Y and R 26, was achieved by illumination in their respective QX bands. Preliminary interpretation of the spectra yields information about the interactions assumed by these molecules in the reaction centers. Spheroidene bound to reaction centers of strain Y probably affects a conformation different from that assumed by the bulk spheroidene of the chromatophore. 相似文献
3.
Purified photochemical reaction centers from Rhodopseudomonas sphaeroides R-26 were reduced with Na2S2O4 so as to block their photochemical electron-transfer reactions. The magnetic field induced an increase in the emission yield. Our results support the hypothesis that under these conditions, charge recombination in the singlet radical pair composed of the oxidized primary donor and reduced primary acceptor predominantly generates the excited singlet state of the reaction center bacteriochlorophyll.The maximum relative fluorescence change and the value of the magnetic field at which half-saturation of the effect is achieved () at room temperature are 5.5% and 75 G, respectively. For the whole cells of Rps. sphaeroides R-26 these parameters are 1.2% and 120 G.The relative fluorescence change at 600 G, , and are studied as functions of temperature. The temperature dependencies of for reaction centers and whole cells of Rps. sphaeroides R-26 are qualitatively the same, with the maximum effect (8% for reaction centers) occurring at 230 K. However, the curves for the two preparations are different. 相似文献
4.
George Britton Harish C. Malhotra Raj Kumari Singh Sandra Taylor Trevor W. Goodwin Avraham Ben-Aziz 《Phytochemistry》1976,15(12):1971-1972
Two new carotenoids isolated from Rhodopseudomonas spheroides (Rhodospirillaceae) have been identified as methoxyspheroidene (1,1′-dimethoxy-3,4-didehydro-1,2,1′,2′,78′-hexahydro-ψ,ψ-carotene) obtained from anaerobic cultures and methoxyspheroidenone (1,1′-dimethoxy-3,4-didehydro-1,2,1′,2′,7′,8′-hexahydro-ψ,ψ-caroten-2-one) recovered from aerobic cultures. 相似文献
5.
The carotenoid-less reaction centers isolated from Rhodopseudomonas sphaeroides (strain R 26) bind pure all-trans spheroidene as well as spheroidenone in a nearly 1:1 molar ratio with respect to P-870. Neither β-carotene nor spirilloxanthin, both absent from wild-type Rps. sphaeroides, could be bound in appreciable amounts. Resonance Raman spectra of the carotenoidreaction center complex indicate that the carotenoid is bound as a cis isomer, its conformation being very close, although probably not identical, to that assumed by the carotenoid in the wild-type reaction centers. The electronic absorption spectra of the carotenoid-reaction center complexes are in good agreement with such a interpretation. When bound to the R 26 reaction centers, spheroidene displays light-induced absorbance changes identical in peak wavelengths and comparable in amplitudes to those observed in the wild-type reaction centers. Thus the binding of the carotenoid to the R 26 reaction centers most likely occurs at the same proteic site as in the wild-type reaction centers. This site shows selectivity towards the nature of carotenoids, and has the same sterical requirement as in the wild type, leading to the observed all-trans to cis isomerisation. 相似文献
6.
The chlorophyll-protein complexes of Acetabularia. A novel chlorophyll complex which forms oligomers
(1) Five minor chlorophyll-protein complexes were isolated from thylakoid membranes of the green alga Acetabularia by SDS-polyacrylamide gel electrophoresis, after SDS or octylglucoside solubilization. None of them were related to CP I (Photosystem I reaction center core) or CP II (chlorophyll light-harvesting complex). (2) Two complexes (CPa-1 and CPa-2) contained only chlorophyll (Chl) a, with absorption maxima of 673 and 671 nm, and fluorescence emission maxima of 683 nm compared to 676 nm for CP II. The complexes had apparent molecular masses of 43–47 and 38–40 kDa, and contained a single polypeptide of 41 and 37 kDa, respectively. They each account for about 3% of the total chlorophyll. (3) Three complexes had identical spectra, with Chl ratios of 3–4 compared to 2 for thylakoid membranes, and a pronounced shoulder around 485 nm indicating enrichment in carotenoids. One of them was the complex ‘CP 29’ (Camm, E.L. and Green, B.R. (1980) Plant Physiol. 66, 428–432) and the other two were slightly different oligomeric forms of CP 29. They could be formed from CP 29 during reelectrophoresis; but about half the complex was isolated originally in an oligomeric form. Together they account for at least 7% of the total chlorophyll. Their function is unknown. 相似文献
7.
Resonance Raman spectroscopy of cytochrome c oxidase and electron transport particles with excitation near the Soret band 总被引:3,自引:0,他引:3
I Salmeen L Rimai D Gill T Yamamoto G Palmer C R Hartzell H Beinert 《Biochemical and biophysical research communications》1973,52(3):1100-1107
We report the resonance Raman spectra of cytochrome oxidase, both solubilized and in electron transport particles using laser excitation near the Soret band. As in the spectra of other hemoproteins, such as cytochrome , the shape and intensity of a number of bands change when the oxidation state is varied. However, one of the hemes of solubilized cytochrome oxidase shows redox behavior which is anomalous. Spectra of electron transport particles are dominated by cytochrome oxidase. There are, however, definite differences between spectra of solubilized cytochrome oxidase and electron transport particles in the oxidized states. 相似文献
8.
The Raman spectrum (441.6 nm excitation) of protocatechuate 3,4-dioxygenase (PCD) from Pseudomonas putida shows resonance enhanced bands at 1605, 1504, 1270, 858, and 830 cm?1 which are due to the p-hydroxyphenyl group of tyrosine coordinated to iron. In addition, we observe strong resonance enhanced bands at 592 and 524 cm?1 and weak (presumably iron-ligand) vibrations at 465, 423, and 371 cm?1. Recent publications of the Raman spectrum of PCD from Pseudomonas aeruginosa (Tatsuno , J. Am. Chem. Soc. 100, 4614–4615 (1978) and Keyes , Biochem. Biophys. Res. Comm. 83, 941–945 (1978) using 488 and 514 nm excitation did not report these bands. Our 441.6 nm excitation Raman spectrum of human serum transferrin, another metalloprotein with an iron-tyrosine linkage, does not show the 592 and 524 cm?1 bands and has only two very weak bands at about 423 and 364 cm?1. We discuss several interpretations of these data. 相似文献
9.
Analysis of photosynthetic reaction centers from Rhodopseudomonas sphaeroides strains 2.4.1 and Ga shows that each contains approx. 1 mol of a specific carotenoid per mol of reaction center. In strain 2.4.1. the carotenoid is spheroidene (1-methoxy-3,4-didehydro-1,2,7′,8′-tetrahydro-ψ,ψ-carotene); in strain Ga, it is chloroxanthin (1-hydroxy-1,2,7′,8′-tetrahydro-ψ,ψ-carotene). The carotenoid is bound to the same pair of proteins as are the bacteriochlorophylls and bacteriopheophytins of the reaction center. This binding induces strong circular dichroism in the absorption bands of the carotenoid. The carotenoid is close enough to the other pigments of the reaction center so that light energy transfers efficiently from the carotenoid to the bacteriochlorophyll, sensitizing bacteriochlorophyll fluorescence. The fluorescence polarization spectrum of the reaction centers shows that the transition vectors for the visible absorption bands of the carotenoid lie approximately parallel to the 600 nm () transition of the bacteriochlorophyll complex. 相似文献
10.
Methods of preparing dried gelatin films containing purified reaction centers of Rhodopseudomonas sphaeroides are described. The spectral properties of reaction centers in solution are essentially maintained in dried gelatin films. These films are uniform and have excellent optical properties, showing little particulate scattering at temperatures down to about 4K. Film contraction on cooling to 90K is less than 1% in linear dimension. Linear dichroism spectra are reported for films at room and low temperature. Reaction centers show a moderate amount of linear dichroism in unstretched gelatin films; the magnitude of the linear dichroism becomes much greater when the films are stretched. In stretched films, linear dichroic ratios (; absorbance measured with electric vector parallel and perpendicular to stretching direction) between 1.7 and 2.2 were obtained for the 860 nm absorption band of the bacteriochlorophyll component that undergoes primary photooxidation. The relative polarizations of light-induced absorption changes of reaction centers in stretched films are similar to those reported by Vermeglio and Clayton ((1976) Biochim. Biophys. Acta 449, 500–515) and support their hypothesis that absorbance decreases, maximal near 860 and 810 nm, and an increase near 790 nm are associated with the respective disappearance and appearance of discrete bands characteristic of the reduced and oxidized bacteriochlorophyll dimer. This interpretation is also supported by the polarization of the absolute absorption spectrum near 810 and 860 nm. An absorption band near 540 nm, ascribed to the Qx transitions of two molecules of bacteriopheophytin in the reaction center, is split at low temperatures into two bands having similar polarizations. This splitting is probably not due to exciton coupling of the two molecules, since excition theory predicts different polarizations. 相似文献
11.
《BBA》1985,810(2):269-273
Comparison of the resonance Raman spectra of carotenoids in vivo and in vitro has revealed that in some species of photosynthetic bacteria the major fraction of carotenoids associated with the light-harvesting systems has forms distorted (twisted) from the planar all-trans conformation. These distorted forms are kept in isolated and purified light-harvesting bacteriochlorophyll-protein complexes. 相似文献
12.
Fluorescence lifetime spectra of Rhodopseudomonas sphaeroides chromatophores have been measured at room temperature by phase fluorimetry at 82 MHz in order to investigate the heterogeneity of the emission. The total fluorescence was decomposed into two main components. A constant component, Fc, centered at 865 nm, represents about 50% of the total emission from dark-adapted chromatophores (Fo) and has a lifetime of 0.55 ns. A variable component is centered at 890 nm. Upon closing the reaction centers, 5-fold increases take place in both emission yield and lifetime of this component. In the dark-adapted state, its lifetime is about 50 ps and its contribution to the total fluorescence is 70% at 890 nm. In the presence of sodium dithionite, a long-lifetime component () is observed. This probably arises from radical pair recombination between P+ and I? (P, the primary electron donor, is a dimer of bacteriochlorophyll; I, the primary electron acceptor, is a molecule of bacteriopheophytin). Its spectrum is nearly identical to that of the variable component. This emission seems to be present also under nonreducing conditions, although with a much weaker intensity than when the electron acceptor quinone is prereduced. 相似文献
13.
Yasushi Koyama Mariko Kito Tomoko Takii Kayoko Saiki Kiyoshi Tsukida Jinpei Yamashita 《BBA》1982,680(2):109-118
The resonance Raman spectrum of the reaction center of Rhodopseudomonas sphaeroides G1C as well as those of the cis-trans isomers of β-carotene (all-trans, 9-cis, 13-cis, 15-cis and 9-cis, 13-cis- (or 9-cis, 13′-cis)) have been recorded at liquid N2 temperature by use of the 457.9, 488.0 and 514.5 nm excitation lines. Comparison of the spectra indicated that the carotenoid in the reaction center takes the 15-cis configuration. 相似文献
14.
The mineral helvite, (Mn4S)(BeSiO4)3, contains discrete tetrahedral Mn4S+6 clusters in which the S?2 is tetrahedrally coordinated and each Mn(II) is in a distorted tetrahedron of one S?2 and three oxygens; the cluster is situated within an encompassing lattice of SiO4?4 and BeO4?6 tetrahedra. Mn4S+6 centers provide an interesting model for comparison to the polynuclear manganese center that is associated with photosynthetic water oxidation. Magnetic susceptibility data between 77 and 298 K have been measured for a natural helvite sample containing principally Mn4S+6 centers but with significant contamination from Mn3FeS+6 and Mn3CaS+6. The data exhibited Curie-Weiss behavior with μeff = 5.969 B.M. and θ = 178.3 K. An analysis of the magnetic susceptibility, based on Van Vleck's formalism, demonstrated the presence of antiferromagnetic coupling, with a coupling constant J = ?5.83 cm?1. Mössbauer spectra of Mn3FeS centers in helvite and of Fe4S centers in the related mineral danalite have also been recorded. Isomer shifts show little temperature dependence and lie in the range 1.23–1.43 . This range is typical of tetrahedrally coordinated Fe(II) in several ionic crystals but is significantly above that of Fe(II) in ferredoxins and below that in the [quinone-Fe(II)-quinone] complex of the photosynthetic bacterium,Rhodopseudomonas sphaeroides. Quadrupole splittings are highly temperature dependent, ranging from 2.4 at 4.2 K to less than 0.5 at 248 K. 相似文献
15.
Low-temperature absorption, circular dichroism and resonance Raman spectra of the LM units isolated with sodium dodecyl sulfate from wild-type Rhodopseudomonas sphaeroides reaction centers (Agalidis, I. and Reiss-Husson, F. (1983) Biochim. Biophys. Acta 724, 340–351) are described in comparison with those of intact reaction centers. In LM unit, the Qy absorption band of P-870 at 77 K shifted from 890 nm (in reaction center) to 870 nm and was broadened by about 30%. In contrast, the 800 nm bacteriochlorophyll absorption band including the 810 species remained unmodified. It was concluded that the 810 nm transition is not the higher excitonic component of P-870. The Qx band of P-870 shifted from 602 nm (in reaction center) to 598 nm in LM, whereas the Qx band of the other bacteriochlorophylls was the same in reaction center and LM and had two components at about 605 and 598 nm. The QxII band of bacteriopheophytin was upshifted to 538 nm and a slight blue shift of the Qy band of bacteriopheophytin was observed. Resonance Raman spectra of spheroidene in LM showed that its native cis-conformation was preserved. Resonance Raman spectroscopy also demonstrated that in LM the molecular interactions assumed by the conjugated carbonyls of bacteriochlorophyll molecules were altered, but not those assumed by the bacteriopheophytins carbonyls. In particular at least one Keto group of bacteriochlorophyll free in reaction center, becomes intermolecularly bounded in LM (possibly with extraneous water). This group may belong to the primary donor molecules. 相似文献
16.
The newly developed technique of resonance Raman spectroelectrochemistry (RRSE) is applied to the study of the radical ion species involved in the primary photochemistry of photosynthesis. By means of controlled potential coulometry combined with resonance Raman spectroscopic detection, the vibrational spectrum of the bacteriochlorophyll cation radical (BChl+·) has been obtained and compared with the corresponding spectrum of the parent molecule. The cation radical spectrum is significantly different from the neutral spectrum both in band frequencies and intensities. These results suggest that RR vibrational spectra may provide a new means of identifying and kinetically monitoring radical ion formation both in photosynthetic model systems and . 相似文献
17.
The structural and functional organization of the spinach chloroplast photosystems (PS) I, IIα and IIβ was investigated. Sensitive absorbance difference spectrophotometry in the ultraviolet (?A320) and red (?A700) regions of the spectrum provided information on the relative concentration of PS II and PS I reaction centers. The kinetic analysis of PS II and PS I photochemistry under continuous weak excitation provided information on the number (N) of chlorophyll (Chl) molecules transferring excitation energy to PS IIα, PS IIβ and PS I. Spinach chloroplasts contained almost twice as many PS II reaction centers compared to PS I reaction centers. The number Nα of chlorophyll (Chl) molecules associated with PS IIα was 234, while Nβ = 100 and NPS I = 210. Thus, the functional photosynthetic unit size of PS II reaction centers was different from that of PS I reaction centers. The relative electron-transport capacity of PS II was significantly greater than that of PS I. Hence, under light-limiting green excitation when both Chl a and Chl b molecules are excited equally, the limiting factor in the overall electron-transfer reaction was the turnover of PS I. The Chl composition of PS I, PS IIα and PS IIβ was analyzed on the basis of a core Chl a reaction center complex component and a Chl component. There is a dissimilar Chl composition in the three photosystems with 77% of total Chl b associated with PS IIα only. The results indicate that PS IIα, located in the membrane of the grana partition region, is poised to receive excitation from a wider spectral window than PS IIβ and PS I. 相似文献
18.
F.C. Pennington F.T. Haxo G. Borch S. Liaaen-Jensen 《Biochemical Systematics and Ecology》1985,13(3):215-219
The carotenoids of selected Cryptophyceae, Rhodomonas D3 and Cryptomonas ovata, have been examined by methods including HPLC, mass spectrometry 1H NMR and circular dichroism. has been assigned to monadoxanthin from 1H NMR and CD data; β,?-carotene possessed the common . The quantitative distribution pattern of carotenoids in Cryptophyceae established here and previously, totalling five species' is discussed in chemosystematic context. β,?-Carotene (3–8% of total) is the major carotene, accompanied by ?,?-carotene (0.2%), β,β-carotene (0–1%) and lycopene (0-trace). Zeaxanthin (2%) was identified in C. ovate. The diacetylenic alloxanthin is the major carotenoid (70–88%), and the monoacetylenic crocoxanthin (5–15%) and monadoxanthin (0–16%) less abundant. No epoxidic or allenic carotenoids could be detected. The biosynthetic precursor of acetylenic carotenoids in this primitive algal class is discussed. The significance of Cryptophyceae in the marine food chain is commented on, using alloxanthin as an indicator. 相似文献
19.
Hans R. Kricheldorf Detlef Müller 《International journal of biological macromolecules》1984,6(3):145-151
In order to study the chemical shifts and the cis—trans isomerism of prolyl units neighbouring glycine or other amino acids, 75.4 MHz13C nuclear magnetic resonance (n.m.r.) cross-polarization/magic angel spinning (CP/MAS) spectra of the following solid oligopeptides and sequence polypeptides were measured: Z-Gly-Pro-OH,Z-Gly-Pro-Gly-Gly-OEt,Z-Gly-Pro-Ala-Ala-OMe,(Gly-Pro-Gly)n,(Gly-Pro-Ala)n,(β-Ala-Pro)n and ). Whereas all these oligo- and polypeptided contain exclusively trans X-Pro bonds, both cis and trans peptide bonds were found in a polypeptide prepared by copolymerization of glycine- and in pyridine. On the basis of these model compounds, the 13C n.m.r. CP/MAS spectra of solid elastin allows the following conclusions. Almost all X-Pro bonds assume the trans conformation, most alanine and leucine units form α-helical chain segments, whereas only a small fraction of β-sheet structure is present. A 30.3 MHz 15N n.m.r. CP/MAS spectrum of solid elastin confirms that ~25% of all amino acids assume the α-helical structure. A model of elastin is discussed consisting of an amorphous phase, α-helical chain segments and helical segments of still unknown pitch. 相似文献
20.
Reaction centers have been purified from chromatophores of Rhodopseudomonas viridis by treatment with lauryl dimethyl amine oxide followed by hydroxyapatite chromatography and precipitation with ammonium sulfate. The absorption spectrum at low temperature shows bands at 531 and 543 nm, assigned to two molecules of bacteriopheophytin b. The 600 nm band of bacteriochlorophyll b is resolved at low temperature into components at 601 and 606.5 nm. At room temperature the light-induced difference spectrum shows a negative band centered at 615 nm, where the absorption spectrum shows only a weak shoulder adjacent to the 600 nm band. The fluorescence spectrum shows a band at 1000 nm and no fluorescence corresponding to the 830 nm absorption band. Two molecules of cytochrome 558 and three of cytochrome 552 accompany each reaction center. The differential extinction coefficient (reduced minus oxidized) of cytochrome 558 at 558 nm was estimated as 20 ± 2 mM?1 · cm?1 through a coupled reaction with equine cytochrome c. The extinction coefficient of reaction centers at 960 nm was determined to be 123 ± 25 mM?1 · cm?1 by measuring the light-induced bleaching of P-960 and the coupled oxidation of cytochrome 558. The corresponding extinction coefficient at 830 nm is 300 ± 65 mM?1 · cm?1. The absorbance ratio in our preparations was 2.1, and there was 190 kg protein per mol of reaction centers. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed three major components of apparent molecular weights 31 000, 37 000 and 41 000. 相似文献