PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Energy Transfer”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

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

At least 37 records · Page 2Linked to original sources
PubMed1978

Enhancement of banding patterns in human metaphase chromosomes by energy transfer.

Intermolecular energy transfer between appropriately chosen pairs of dyes can be used to induce or enhance banding patterns in human metaphase chromosomes. Energy transfer, calibrated by fluorometric studies on soluble dye.DNA complexes, can also be detected by photometric measurements on cytological preparations of metaphase chromosomes stained with pairs of fluorochromes. If a fluorescent dye with one type of binding or quantum yield specificity (e.g., quinacrine, 33258 Hoechst, or chromomycin A(3)) is employed together with a counterstain (e.g., actinomycin D, 7-aminoactinomycin D, or methyl green) exhibiting a complementary base pair binding specificity and satisfying spectral overlap criteria for energy transfer, contrast in fluorescence from the first dye is enhanced in specific subsets of standard chromosome bands. Extensive energy transfer presumably suppress donor fluorescence except in chromosomal region containing clusters of at least 20 base pairs predominantly of one type, within which the donor but not the acceptor can bind and fluoresce. Quinacrine-bright polymorphic regions are especially resistant to fluorescence quenching by counterstains with G.C binding specificity, strengthening the evidence that these latter regions are highly enriched for A.T base pair clusters. The ability to highlight selectively many such polymorphic regions may prove of further, practical, utility in a number of cytogenetic problems.

Chromosomes, Human↗
PubMed1991

Phosphoinositide-protein interactions of the plasma-membrane Ca2(+)-transport ATPase as revealed by fluorescence energy transfer.

Fluorescence energy transfer has been used to study the interaction of various phospholipids with the erythrocyte (Ca2+ + Mg2+)-ATPase. The fluorescence energy transfer between tryptophan residues of the (Ca2+ + Mg2+)-ATPase purified from erythrocytes and pyrene-labelled analogues of phosphatidylcholine (Pyr-PC), phosphatidylinositol (Pyr-PI), phosphatidylinositol 4-phosphate (Pyr-PIP), phosphatidylinositol 4,5-bisphosphate (Pyr-PIP2), phosphatidylglycerol (Pyr-PG) and phosphatidic acid (Pyr-PA) was measured. A positive correlation was found between the number of negative charges on the phospholipids (PIP2 greater than PIP greater than PA greater than PI = PG greater than PC) and the potency of their pyrene-labelled analogues to act as quantum acceptors in fluorescence energy transfer from the tryptophan residues of the (Ca2+ + Mg2+)-ATPase. This is the first time that a physical interaction between PIP/PIP2 and an intrinsic membrane protein has been demonstrated. The dependence of the energy transfer on the number of negative charges of the phospholipids closely resembles the previously demonstrated charge dependence of the enzymatic activity of the (Ca2+ + Mg2+)-ATPase (Missiaen, L., Raeymaekers, L., Wuytack, F., Vrolix, M., Desmet, H. and Casteels, R. (1989) Biochem. J. 263, 687-694). It is concluded that the stimulation of the (Ca2+ + Mg2+)-ATPase activity by negatively charged phospholipids is based on a binding of these lipids to the (Ca2+ + Mg2+)-ATPase and that the negative charges are a major modulatory factor for this interaction.

Animals↗
PubMed1986

A homogeneous assay for biotin based on chemiluminescence energy transfer.

Chemiluminescence energy transfer between aminobutylethylisoluminol (ABEI)-biotin and fluorescein-avidin was investigated in order to establish a homogeneous assay for serum biotin in the physiological range. ABEI chemiluminescence was measured at pH 7.4 using microperoxidase-hydrogen peroxide and the chemiluminescence at two wavelengths (460 and 525 nm) measured simultaneously to quantify chemiluminescence energy transfer. ABEI-biotin was synthesized by a mixed anhydride reaction and purified by TLC and HPLC. Binding of ABEI-biotin to fluorescein-avidin resulted in a quenching of the chemiluminescence. Chemiluminescence energy transfer was demonstrated by a 2.5-fold decrease in the ratio of blue (460 nm) to green (525 nm) light emission compared with unbound ABEI-biotin. This energy transfer was used to establish an assay for biotin in the range 1 to 10 nM by relating the concentration of biotin to the ratio of chemiluminescence monitored at 460 and 525 nm simultaneously. The assay was capable of detecting biotin in reference sera and in patients with malabsorption syndromes and chronic alcoholism. The reference range in normal subjects was 1.2 to 4.3 nmol/liter mean +/- SD = 2.41 +/- 0.91 nmol/liter (n = 20). The quenching of the chemiluminescence of ABEI-biotin when bound to fluorescein-avidin appeared to be the result of a direct interaction between the excited state product of ABEI and fluorescein.

Avidin↗
PubMed1990

Electrostatic field around cytochrome c: theory and energy transfer experiment.

Energy transfer in the "rapid diffusion" limit from electronically excited terbium(III) chelates in three different charge states to horse heart ferricytochrome c was measured as a function of ionic strength. Theoretical rate constants calculated by numerical integration of the Forster integral (containing the Poisson-Boltzmann-generated protein electrostatic potential) were compared with the experimental data to evaluate the accuracy of protein electrostatic field calculations at the protein/solvent interface. Two dielectric formalisms were used: a simple coulombic/Debye-Hückel procedure and a finite difference method [Warwicker, J. & Watson, H. C. (1982) J. Mol. Biol. 157, 671-679] that accounts for the low-dielectric protein interior and the irregular protein/solvent boundary. Good agreement with experiment was obtained and the ionic-strength dependence of the reaction was successfully reproduced. The sensitivity of theoretical rate constants to the choices of effective donor sphere size and the energy transfer distance criterion was analyzed. Electrostatic potential and rate-constant calculations were carried out on sets of structures collected along two molecular dynamics trajectories of cytochrome c. Protein conformational fluctuations were shown to produce large variations in the calculated energy transfer rate constant. We conclude that protein fluctuations and the resulting transient structures can play significant roles in biological or catalytic activities that are not apparent from examination of a static structure. For calculating protein electrostatics, large-scale low-frequency conformational fluctuations, such as charged side-chain reorientation, are established to be as important as the computational method for incorporating dielectric boundary effects.

Animals↗
PubMed2006

Photoinduced electron transfer and excitation energy transfer in directly linked zinc porphyrin/zinc phthalocyanine composite.

Photoinduced electron transfer (ET) and excitation energy transfer (ENT) reactions in monomer and slipped-cofacial dimer systems of a directly linked Zn porphyrin (Por)-Zn phthalocyanine (Pc) heterodyad, ZnPc-ZnPor, were investigated by means of the picosecond and femtosecond transient absorption spectroscopies. In the dimer dyad system of two heterodyads connected through the coordination bond between two imidazolyl-substituted ZnPor bearing ZnPc, ZnPc-ZnPor(D), the rapid ENT from the ZnPor to ZnPc in the subpicosecond time region was followed by photoinduced charge separation (CS) and charge recombination (CR) with time constants of 47 and 510 ps, respectively. On the other hand in the monomer dyad system, no clear charge-separated state was observed although the CS with a time constant of 200 ps and CR with < or =70 ps were estimated. These results indicated that the dimer slipped-cofacial arrangement of pair porphyrins is advantageous for the effective production of the CS state. This advantage was discussed from the viewpoint of a decrease in the reorganization energy of the dimer relative to that of the monomer system. In addition, the electrochemical measurements indicated that the strong interaction between ZnPc and ZnPor moieties also contributed to the fast CS process despite the marginal driving force for the CS process. The dimer dyad of ZnPc-ZnPor provides full advantages in efficiencies of the light harvesting and the CS state production.

Journal Article↗
PubMed2006

Energy transfer between biological membranes.

The crystal structures of two transport proteins associated with a fragment of the TonB protein have been reported for the first time in two recent papers. TonB is implicated in transferring energy from the cytoplasmic membrane to the outer membrane of Gram-negative bacteria. The very similar structures of the protein complexes define the mode of interactions of TonB with active transport proteins.

Bacterial Outer Membrane Proteins↗
PubMed2005

Kinetics of fluorescence quenching for electron transfer and for energy transfer: molecular dynamics tests for spherical molecules.

The Smoluchowski approach to description of fluorescence quenching is tested by comparing the theory with computer simulations for the case of spherical molecules. The distance dependent sink terms describing the electron transfer mechanism and the Forster model for the energy transfer are considered. It is shown that the agreement between the rate coefficient from the model and from simulations depends on the strength of the solute-solvent interactions as well as on the speed of reaction itself. Comparing results of simulations for different quencher concentrations we estimate the strength of quencher concentration dependence effect and the range of times the effect may be significant. In the long time limit the increase in quencher concentration decreased the rate coefficient.

Journal Article↗
PubMed1999

Structure of cytochrome c complexes with phospholipids as revealed by resonance energy transfer.

Resonance energy transfer between a series of lipid-bound fluorescent probes as donors and the heme group of cytochrome c as acceptor has been used to obtain structural information on the protein complexes with model membranes, composed of phosphatidylcholine and cardiolipin. Analysis of experimental data in terms of the model of energy transfer in two-dimensional systems provides further evidence for preferential cytochrome c orientation with respect to the lipid bilayer and penetration of the protein into the membrane interior.

Animals↗
PubMed1980

Proximity of antibody binding sites studied by fluorescence energy transfer.

Fluorescence energy transfer experiments by steady-state and nanosecond monophoton techniques were carried out with a covalently linked hybrid rabbit IgG antibody containing one antilactose site and one anti-Dns [5-(dimethylamino)-1-naphthalenesulfonyl] site. The hybrid antibody was prepared from antilactose and anti-Dns antibody by mild reduction, dissociation into half-molecules in acid, and random reassociation with re-formation, to the extent of 80%, of the single disulfide bond between the heavy chains. Fractionation with an antilactose-specific immunoadsorbent yielded a population in which each IgG molecule contained no more than one anti-Dns site per antibody. The acceptor molecules used for intramolecular energy transfer were derivatives of p-aminophenyl beta-lactoside (PAPL): (dimethyl-amino)benzeneazo-PAPL and N-fluorescyl-PAPL. The fluorescence lifetime (24 ns) and quantum yield (0.57) of the bound Dns group were unaffected by the presence of the acceptor in the adjacent site. Three models were used to calculate the minimum distance between the adjacent sites of the IgG antibody based on the overlap in the emission and absorption spectra of the donor-acceptor pairs and the segmental flexibility of the immunoglobulin molecule. The calculations yielded values in the range of 5.5-7.0 nm for the minimum distance of separation between the antibody sites in solution and demonstrated a substantial energy barrier to the closer approach of the sites.

Animals↗
PubMed1989

Rhodopsin-G-protein interactions monitored by resonance energy transfer.

Resonance energy transfer measurements were implemented to monitor the specific interactions between G-protein and rhodopsin in phospholipid vesicles reconstituted with the purified proteins. Fluorescently labeled G-protein was extracted from bleached rod outer segments (ROS) reacted with several sulfhydryl reagents: N-(1-pyrenyl)maleimide (P), monobromobimane (B), 7-(diethylamino)-3-(4-maleimidylphenyl)-4-methylcoumarin (C), and N-(4-anilino-1-naphthyl)maleimide (A). Limited labeling of ROS, resulting in the modification of less than a single -SH residue per G-protein molecule and less than 0.2 residue per rhodopsin, did not impair the specific in situ interactions between rhodopsin and G-protein. This was demonstrated by preservation of their light-activated tight association and Gpp(NH)p binding and their fast dissociation with excess GTP. The distribution of fluorescent label among the three subunits of G-protein revealed a highly reactive -SH group in the gamma subunit accessible to labeling when G-protein was bound specifically to bleached rhodopsin. Recombination of purified fluorescent derivatives of G-protein with purified rhodopsin reconstituted in lipid vesicles restored the light-activated Gpp(NH)p binding to a level comparable to that measured with unlabeled G-protein. Similar observations were obtained with ROS depleted of peripheral proteins. Likewise, modification of up to two -SH groups per rhodopsin molecule with the fluorescent reagents did not affect the functional recombination of G-protein with rhodopsin in reconstituted lipid vesicles or in depleted ROS. Interactions between rhodopsin and G-protein were monitored by resonance energy transfer measurements, with the following fluorescent conjugates as donor/acceptor couples: P-rhodopsin/C-G-protein, P-rhodopsin/B-G-protein, and P-G-protein/C-rhodopsin.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1981

Detection of actin assembly by fluorescence energy transfer.

Fluorescence energy transfer was used to measure the assembly and disassembly of actin filaments. Actin was labeled at cysteine 373 with an energy donor (5-iodoacetamidofluorescein) or an energy acceptor (tetramethylrhodamine iodoacetamide or eosin iodoacetamide). Donor-labeled actin and acceptor-labeled actin were coassembled. The dependence of the transfer efficiency on the mole fraction of acceptor-labeled actin showed that the radial coordinate of the label at cysteine 373 is approximately 35 A, which means that this site is located near the outer surface of the filament. The distance between a donor and the closest acceptor in such a filament is 58 A. The increase in fluorescence after the mixing of actin filaments containing both donor and acceptor with unlabeled filaments showed that there is a slow continuous exchange of actin units. The rate of exchange was markedly accelerated when the filaments were sonicated. The rapid loss of energy transfer caused by mechanical shear probably resulted from an increase in the number of filament ends, which in turn accelerated the exchange of monomeric actin units. Energy transfer promises to be a valuable tool in characterizing the assembly and dynamics of actin and other cytoskeletal and contractile proteins in vitro and in intact cells.

Actins↗
PubMed2001

Photoinduced electron transfer and electronic energy transfer in naphthyl-appended cyclams.

A series of novel macrocyclic tetraaza ligands that incorporate a naphthalene moiety as a photoactive chromophore have been prepared and structurally characterized as their Cu(II) complexes. Variable-temperature photophysical studies have concluded that the luminescence quenching evident in the Cu(II) complexes is due to intramolecular electronic energy transfer (EET). In their free-base forms, these ligands undergo reductive luminescence quenching via photoinduced electron transfer (PET) reactions, with proximate amine lone pairs acting as electron donors. Consequently, the emission behavior can be modulated by variations in pH and/or the presence of other Lewis acids such as Zn(II).

Journal Article↗
PubMed1977

Application of radiationless energy transfer for distance measurements across membranes. Transition Probabilities for radiationless energy transfer within several assemblies of donors and acceptors at stationary distances.

For several 2-or 3-dimensional configurations of stationary donors and acceptors on or near a spherical membrane shell the transition probabilities for radiationless energy transfer are calculated, using Förster's approximation obtained for Coulombic dipole-dipole interaction of the transition moments. It turns out that the difference in the refractive indices for membrane (lipid) and bulk phase (water) has only a small influence on the transition probabilities. Furthermore, the curvature of biological cell surfaces can be neglected, but affects the energy transfer across small vesicles. The ratio thickness/radius of small vesicles can be determined by measuring fluorescence quenching of excited donors by acceptors on the other side of the membrane.

Energy Transfer↗
PubMed1992

Distance distribution in a dye-linked oligonucleotide determined by time-resolved fluorescence energy transfer.

Fluorescence energy transfer is potentially a useful technique for obtaining structural and dynamic information on duplex and branched DNA molecules suitably labeled with donor and acceptor dyes. We have assessed the accuracy and limitations of FET measurements in nucleic acids with respect to the localization of the dyes and the flexibility of the dye-DNA linkages. A nine base-pair duplex oligonucleotide was synthesized with donor and acceptor dyes linked at the opposing 5' termini by alkyl chains. A careful analysis of the fluorescence decay of the donor revealed that the donor-acceptor distance in this molecule was not well defined, but was described by a rather broad distribution. The mean donor-acceptor distance and the distribution of distances have been recovered from the donor decay. Orientational effects on energy transfer have been included in the analysis. The implications of these findings for FET measurements in nucleic acids are considered.

Base Sequence↗
PubMed2005

Photoinduced electron transfer competitive with energy transfer of the excited triplet state of [60]fullerene to ferrocene derivatives revealed by combination of transient absorption and thermal lens measurements.

The quenching processes of the exited triplet state of fullerene (3C60) by ferrocene (Fc) derivatives have been observed by the transient absorption spectroscopy and thermal lens methods. Although 3C60 was efficiently quenched by Fc in the rate close to the diffusion controlled limit, the quantum yields (phi(et)) for the generation of the radical anion of C60 (C60*-) via 3C60 were quite low even in polar solvents; nevertheless, the free-energy changes (deltaG(et)) of electron transfer from Fc to 3C60 are sufficiently negative. In benzonitrile (BN), the phi(et) value for unsubstitued Fc was less than 0.1. The thermal lens method indicates that energy transfer from 3C60 to Fc takes place efficiently, suggesting that the excited triplet energy level of Fc was lower than that of 3C60. Therefore, energy transfer from 3C60 to ferrocene decreases the electron-transfer process from ferrocene to 3C60. To increase the participation of electron transfer, introduction of electron-donor substituents to Fc (phi(et) = 0.46 for decamethylferrocene in BN) and an increase in solvent polarity (phi(et) = 0.58 in BN:DMF (1:2) for decamethylferrocene) were effective.

Journal Article↗
PubMed2005

Fluorescence energy transfer methods in bioanalysis.

Energy transfer phenomena, in which excited fluorophores transfer energy to neighbouring chromophores, are well characterised in photochemistry and have found a wide range of applications in analytical biochemistry. The transfer of energy from a donor to an acceptor group is only significant over distances of a few nm, so it can be used as a spectroscopic ruler and as a means of detecting molecular interactions and conformational changes. Such methods usually retain the great sensitivity and sample handling flexibility of conventional fluorescence techniques. As a result many assays involving enzymes, antibodies and nucleotides utilise energy transfer measurement principles. This article outlines these principles for the main types of energy transfer, and summarises some of their most important areas of application.

Energy Transfer↗
PubMed1990

A determination of the radial coordinate of Tyr-69 in F-actin using fluorescence energy transfer.

Fluorescence energy transfer was measured between Tyr-69 residues in an F-actin filament using 5-dimethylaminonaphthalene-1-sulfonyl chloride (DNS-Cl) as a fluorescence energy donor and 4-dimethylaminoazobenzene-4-sulfonyl chloride (DABSYL-Cl) as the acceptor. Both labels are covalently attached to Tyr-69 residues in an F-actin filament. Taking the helical structure of the F-actin filament into consideration, the radial coordinate of Tyr-69 was calculated to be in the range from 2.0 nm to 4.0 nm.

Actins↗