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1.
Dynamic Light Regulation of Photosynthesis (A Review) 总被引:9,自引:7,他引:2
Regulatory reactions providing the photosynthetic apparatus with the ability to respond to variations of irradiance by changes in activities of the light and the dark stages of photosynthesis within a time range of seconds and minutes are considered in the review. At the light stage, such reactions are related to the changes in both distribution of light energy between two photosystems and probability of nonphotochemical dissipation of absorbed quanta in PSI and PSII. These regulatory reactions operate in a negative feedback mode, thus avoiding overreduction of electron transport chain and minimizing the probability of generation of reactive oxygen species. The crucial role in preventing the generation of reactive oxygen species belongs to dynamic regulation of electron transport activity despite the presence of complex system of their detoxification in chloroplasts. In dark reactions of Calvin cycle, the regulatory responses involve a positive feedback principle being related to redox regulation of activities of several enzymes, which is sensitive to the reduction status of PSI acceptor side. The complex of regulatory reactions based on negative and positive feedback principles provides prolonged functioning of a chloroplast and high stability of photosynthetic activity under various light conditions. 相似文献
2.
3.
The protolytic reactions of PSII membrane fragments were analyzed by measurements of absorption changes of the water soluble indicator dye bromocresol purple induced by a train of 10 s flashes in dark-adapted samples. It was found that: a) in the first flash a rapid H+-release takes place followed by a slower H+-uptake. The deprotonation is insensitive to DCMU but is completely eliminated by linolenic acid treatment of the samples; b) the extent of the H+-uptake in the first flash depends on the redox potential of the suspension. In this time domain no H+-uptake is observed in the subsequent flashes; c) the extent of the H+-release as a function of the flash number in the sequence exhibits a characteristic oscillation pattern. Multiphasic release kinetics are observed. The oscillation pattern can be satisfactorily described by a 1, 0, 1, 2 stoichiometry for the redox transitions Si Si+1 (i=0, 1, 2, 3) in the water oxidizing enzyme system Y. The H+-uptake after the first flash is assumed to be a consequence of the very fast reduction of oxidized Q400(Fe3+) formed due to dark incubation with K3[Fe(CN)6]. The possible participation of component Z in the deprotonation reactions at the PSII donor side is discussed.Abbreviations A
protonizable group at the PSII acceptor side
- BCP
Bromocresol Purple
- DCMU
3-(3,4-dichlorophenyl)-1,1-dimethylurea
- FWHM
Full Width at Half Maximum
- QA, QB
primary and secondary plastoquinone at PSII acceptor side
- Q400
redox group at PSII-acceptor side (high spin Fe2+)
- P680
Photoactive chlorophyll of PSII reaction center
- Si
redox states of the catalytic site of water oxidation
- Z
redox component connecting the catalytic site of water oxidation with the reaction center 相似文献
4.
Summary Nonstationary pump currents which have been observed in K+-free Na+ media after activation of the Na,K-ATPase by an ATP-concentration jump (see the preceding paper) are analyzed on the basis of microscopic reaction models. It is shown that the behavior of the current signal at short times is governed by electrically silent reactions preceding phosphorylation of the protein; accordingly, the main information on charge-translocating processes is contained in the declining phase of the pump current. The experimental results support the Albers-Post reaction scheme of the Na,K-pump, in which the translocation of Na+ precedes translocation of K+. The transient pump current is represented as the sum of contributions of the individual transitions in the reaction cycle. Each term in the sum is the product of a net transition rate times a dielectric coefficient describing the amount of charge translocated in a given reaction step. Charge translocation may result from the motion of ion-binding sites in the course of conformational changes, as well as from movement of ions in access channels connecting the binding sites to the aqueous media. A likely interpretation of the observed nonstationary currents consists in the assumption that the principal electrogenic step is the E1-P/P-E2 conformational transition of the protein, followed by a release of Na+ to the extracellular side. This conclusion is supported by kinetic data from the literature, as well as on the finding that chymotrypsin treatment which is known to block the E1-P/P-E2 transition abolishes the current transient. By numerical simulation of the Albers-Post reaction cycle, the proposed mechanism of charge translocation has been shown to reproduce the experimentally observed time behavior of pump currents. 相似文献
5.
Heterotrimeric guanine nucleotide-binding regulatory proteins (G proteins) serve to transduce information from agonist-bound receptors to effector enzymes or ion channels. Current models of G protein activation-deactivation indicate that the oligomeric GDP-bound form must undergo release of GDP, bind GTP and undergo subunit dissociation, in order to be in active form (GTP bound subunits and free dimers) and to regulate effectors. The effect of receptor occupation by an agonist is generally accepted to be promotion of guanine nucleotide exchange thus allowing activation of the G protein. Recent studies indicate that transphosphorylation leading to the formation of GTP from GDP and ATP in the close vicinity, or even at the G protein, catalysed by membrane-associated nucleoside diphosphate kinase, may further activate G proteins. This activation is demonstrated by a decreased affinity of G protein-coupled receptors for agonists and an increased response of G protein coupled effectors. In addition, a phosphorylation of G protein subunits and consequent phosphate transfer reaction resulting in G protein activation has also been demonstrated. Finally, endogenously formed GTP was preferentially effective in activating some G proteins compared to exogenous GTR The aim of this report is to present an overview of the evidence to date for a transphosphorylation as a means of G protein activation (see also refs [1 and 2] for reviews). (Mol Cell Biochem 157: 593, 1996)Recipient of Servier Investigator Award 相似文献
6.
Three routes were investigated for the conversion of d-glucose into the title compound. In the first approach, reduction of the 5,6-thürane ring of 5,6-dideoxy-5,6-epithio-1,2-O-isopropylidene α-d-glucofuranose (17) as well as that of its 3-O-allyl derivative (13) with lithium aluminium hydride was investigated; 17 afforded the corresponding 6-deoxy derivative besides di-, tri-, and poly-mers, whereas only polymers were formed from 13. In the second approach, the oxirane ring of was reduced by sodium borohydride and the resulting 6-deoxy derivative was converted into the 5-thiobenzoate; the corresponding hex-4-enofuranose was formed as a byproduct. In the third approach partial mesylation of methyl 5-thio-α-d-glucopyranoside was attempted, but the 6-mesylate 27 could be isolated only in modest yield (28%) together with rearranged 2,5-thioanhydromannofuranoside derivatives. The mechanism of this rearrangement is discussed in detail. The 6-mesylate 27 was converted via the 6-iodo derivative into the title compound. 相似文献
7.
C. Kevers B. Bisbis F. Le Dily J. P. Billard C. Huault Th. Gaspar 《In vitro cellular & developmental biology. Plant》1995,31(2):122-126
The transfer of light-cultured green normal (N) and white habituated (HNO) sugarbeet callus to darkness reduced the growth
of N callus and improved growth and delayed necrosis in the HNO callus. The decrease of dry matter of N callus under darkness
was accompanied by a reduced content of carotenoids and by decreased CO2 fixation, which was compensated by an increased dependency on externally supplied sucrose. The levels of some organic nitrogen
compounds such as glutamate, proline, and free polyamines were not affected by transfer to darkness of N or HNO callus. Darkness
decreased ethylene emissions in both callus types. In the HNO callus, the sucrose growth dependency and the CO2 fixation were unaffected by darkness. Chlorophylls were absent both in light and darkness, whereas some carotenoids were
accumulated in the HNO callus only in dark conditions. In another connection, a significant increase of peroxidase activity,
which did not occur in the N callus, was induced by darkness in the HNO callus. A decreased content of thio-barbituric acid
(TBA)-reactive substances was measured in the HNO callus transferred to darkness, whereas an increase was noticed in the N
callus placed in the same conditions. These metabolic changes and the reduction of cellular damage in darkness revealed light-induced
stress reactions leading to necrosis and to reduced growth of HNO callus. It appeared that darkness allowed the HNO callus
to avoid the photooxidation stress. Therefore, the favorable effect of darkness on HNO growth might be explained by the suppression
of photooxidative damage due to the absence of carotenoids. The higher peroxidase activity in the HNO callus maintained in
darkness raised the problem of heme synthesis in this heterotrophic callus. 相似文献
8.
Hydrogen peroxide-mediated inactivation of microsomal cytochrome P450 during monooxygenase reactions
Cytochrome P450 can undergo inactivation following monooxygenase reactions in liver microsomes of untreated, phenobarbital and 3-methylcholanthrene-treated rats and rabbits. The acceleration of cytochrome P450 loss in the presence of catalase inhibitors (sodium azide, hydroxylamine) indicates that hydrogen peroxide is involved in hemoprotein degradation. It was revealed that cytochrome P450 is inactivated mainly by H2O2 formed through peroxy complex breakdown, whereas H2O2 formed via the dismutation of superoxide anions produces a slight inactivating effect. The hydrogen peroxide added outside or formed by a glucose-glucose oxidase system has less of an inactivating effect than H2O2 produced within the cytochrome P450 active center. Self-inactivation of cytochrome P450 during oxygenase reactions is highly specific. Other components of the monooxygenase system, such as cytochrome b5, NADH- and NADPH-specific flavorproteins, undergo no inactivation. The alterations in phospholipid content and in the rate of lipid peroxidation were not observed as well. The inactivation of cytochrome P450 by H2O2 is the result of heme loss or destruction without cytochrome P420 formation. Such. a mechanism operates with different substrates and cytochrome P450 species catalyzing the partially coupled monooxygenase reactions. 相似文献
9.
Raffaello Romeo Giuseppe Arena Luigi Mons Scolaro Maria Rosario Plutino 《Inorganica chimica acta》1995,240(1-2):81-92
The rates of displacement of dimethyl sulfoxide from the cation [Pt(phen) (CH3) (Me2SO)]+ by a series of uncharged and negatively charged nucleophiles have been measured in a methanol/water (19:1 vol./vol.) mixture. The starting complex and the reaction products were characterized either as solids or in solution by their IR and 1H NMR spectra. The substitution reactions take place by way of a direct bimolecular attack of the ligand on the substrate. The sequence of reactivity observed is as expected on the basis of a nucleophilicity scale relevant for + 1 charged substrates ([Pt(en) (NH3)Cl]+ used as standard). The difference of reactivity between the first (t-BuNH2) and the last (SeCN−) members of the series spans five orders of magnitude. The value measured for the nucleophilic discrimination (1.55) is the highest found so far for cationic substrates. This is a result of the easy transfer of some of the electron density brought in by the incoming ligand into the ancillary ligands. When the reaction is carried out in a series of protic and dipolar aprotic solvents, using chloride ion as nucleophile, the rate of formation of [Pt (phen) (CH3)Cl] is dominated by the extent of solvation of Cl−, as measured by its values of the Gibbs molar energy of transfer ΔtG0. Conductivity measurements at 25°C in dichloromethane were fitted to the Fuoss equation and the values of the dissociation constants Kd for the ion pairs were calculated as follows: 2.27 × 10−5 M for Bu4NCl, 2.75 × 10−5 M for Bu4NSCN and 17.05 × 10−5 M for [Pt(phen) (CH3) (Me2SO)]PF6. The pseudo-first-order rate constants kobs for the reactions with Bu4NCl, Bu4NBr, Bu4NSCN and Bu4NI showed a curvilinear dependence on the concentration of the salt which levels off very soon (at concentrations higher than 0.005 M the kinetics are zero order in [Bu4NX]). On addition of the inert electrolyte Bu4NPF6 the rates slow down and the kinetics follow the rate law kobs = kKip[Bu4NX]/[Bu4NPF6] + Kip[Bu4NX]). These findings fit well with a reaction scheme which involves a pre-equilibrium Kip between ion pairs, followed by unimolecular substitution within the contact ion pair [Pt(phen) (CH3) (Me2SO)X]ip. Values of the equilibrium constants Kip for ion-pair exchange and of the internal substitution rates k were derived. The latter showed that the discrimination in reactivity between Cl−, Br−, SCN− and I− is greatly reduced with respect to aqueous solutions. The reason behind this may be desolvation of the ions coupled to the fact that a contact ion pair is already at a certain distance along the reaction coordinate in the direction of the transition state. Applications of the special salt effect and of ion pairing to synthesis are discussed. 相似文献
10.
In the presence of Cl?, the severity of ammonia-induced inhibition of photosynthetic oxygen evolution is attenuated in spinach thylakoid membranes (Sandusky, P.O. and Yocum, C.F. (1983) FEBS Lett. 162, 339–343). A further examination of this phenomenon using steady-state kinetic analysis suggests that there are two sites of ammonia attack, only one of which is protected by the presence of Cl?. In the case of Tris-induced inhibition of oxygen evolution only the Cl? protected site is evident. In both cases the mechanism of Cl? protection involves the binding of Cl? in competition with the inhibitory amine. Anions (Br? and NO?3) known to reactive oxygen evolution in Cl?-depleted membranes also protect against Tris-induced inhibition, and reactivation of Cl?-depleted membranes by Cl? is competitively inhibited by ammonia. Inactivation of the oxygen-evolving complex by NH2OH is impeded by Cl?, whereas Cl? does not affect the inhibition induced by so-called ADRY reagents. We propose that Cl? functions in the oxygen-evolving complex as a ligand bridging manganese atoms to mediate electron transfer. This model accounts both for the well known Cl? requirement of oxygen evolution, and for the inhibitory effects of amines on this reaction. 相似文献