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PubMed1979

Energy transfer in lipid bilayers.

The quenching of fluorescence due to energy transfer between a dilute, random array of donor and acceptor chromophores in lipid bilayer was measured and compared to theoretical expressions developed to predict the decrease in emission intensity under these circumstances. The observed intensity was found to be the same function of quencher concentration in both planar, multilamellar dispersions and small, spherical vesicles. The degree of quenching was accurately predicted by a simple relation derived in this paper, as well as a more complex equation previously developed by Tweet, et al. The results suggest that significant quenching may be observed even when the average donor-acceptor separation exceeds the Förster critical distance by severalfold. Application of these results to problems of current interest in membrane research are discussed.

Energy Transfer↗
PubMed1977

Excitation energy transfer in the light-harvesting chlorophyll a/b.protein.

The "light-harvesting chlorophyll a/b.protein" described by Thornber has been prepared electrophoretically from spinach chloroplasts. The optical properties relevant to energy transfer have been measured in the red region (i.e. 600-700 nm). Measurements of the absorption spectrum, fluorescence excitation spectrum and excitation dependence of the fluorescence emission spectrum of this protein confirm that energy transfer from chlorophyll b to chlorophyll a is highly efficient, as is the case in concentrated chlorophyll solutions and in vivo. The excitiation dependence of the fluorescence polarization shows a minimum polarization of 1.9% at 650 nm which is the absorption maximum of chlorophyll b in the protein and rises steadily to a maximum value of 13.8% at 695 nm, the red edge of the chlorophyll a absorption band. Analysis of these measurements shows that at least two unresolved components must be responsible for the chlorophyll a absorption maximum. Comparison of polarization measurements with those observed in vivo shows that most of the depolarization observed in vivo can take place within a single protein. Circular dichroism measurements show a double structure in the chlorophyll b absorption band which suggest an exciton splitting not resolved in absorption. Analysis of these data yields information about the relative orientation of the So leads to S1 transition moments of the chlorophyll molecules within the protein.

Chlorophyll↗
PubMed1978

Fluorescence energy transfer between epsilon-ATP at the nucleotide binding site and N-(4-dimethylamino-3,5-dinitrophenyl)-maleimide at Cys-373 of G-actin.

The method of fluorescence energy transfer is used to measure the distance from the nucleotide binding site to Cys-373 of G-actin. The fluorescent ATP analogue 1-N6-ethenoadenosine 5'-triphosphate was used as donor and N-(4-dimethylamino-3,5-dinitrophenyl)-maleimide was used as acceptor. From the measurements of the efficiency of fluorescence energy transfer by both static and time resolved fluorometries, the distance between nucleotide binding site and Cys-373 residue of G-actin was calculated to be about 30 A.

Actins↗
PubMed1979

Conformation change in reconstituted thin filament studied with fluorescence energy transfer between epsilon-ADP bound to F-actin and NBD-Cl bound to troponin-C.

The interaction of troponin and F-actin was studied by the methods of fluorescence energy transfer. We used epsilon-ADP bound to F-actin as a fluorescence donor and 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole bound to troponin-C in troponin as a fluorescence acceptor. The efficiency of the fluorescence energy transfer of this system was larger in the absence of calcium ion than in the presence of calcium ion. This shows that the interaction of troponin with F-actin changes in response to the concentration of calcium ion.

4-Chloro-7-nitrobenzofurazan↗
PubMed1979

An analytic solution to the Förster energy transfer problem in two dimensions.

An analytic solution of the Förster energy transfer problem in two dimensions is presented for the case in which the orientation factor is independent of the donor-acceptor distance, and both the donors and acceptors are randomly distributed in a plane. A general solution based on the method of Förster is possible since all distances are measured in units of R0. The analytic solution is extended to the cases of donors embedded in structures that exclude acceptors, and donors that bind acceptors. The validity of the analytic solutions is demonstrated by comparison with numerical simulation calculations. Numerical approximations to the exact solutions are given for ease of computation. Specific applications to the case of fluorescence quenching of a membrane-bound donor by membrane-bound acceptors are presented.

Energy Transfer↗
PubMed1979

Proximity of lectin receptors on the cell surface measured by fluorescence energy transfer in a flow system.

Molecules of the lectin concanavalin A have been labeled separately with the fluorescein and rhodamine chromophores and jointly bound to the surface of transformed Friend erythroleukemia cells. The two dyes constitute an ideal donor-acceptor pair for fluorescence resonance energy transfer thereby permitting the determination of the proximity relationships between bound ligand molecules and the corresponding surface receptors. The transfer efficiency at saturation (about 57%) was measured in a multiparameter flow system using laser excitation at 488 nm and detection of fluorescein and rhodamine emission intensities as well as the emission anisotropy of the rhodamine fluorescence for each cell. The degree of energy transfer was estimated from the quenching of donor emission, the sensitization of acceptor emission, and the depolarization of acceptor fluorescence. The system has been modeled according to a formalism developed by Gennis and Cantor (Biochemistry 11: 2509, 1972). We estimate the separation between the surfaces of bound lectin molecules at saturation to be 0-40 A, a range possibly characteristic for micropatches induced by ligand binding.

Animals↗
PubMed1979

Energy transfer and regional blood flow changes following missile trauma.

The hemodynamic response to missile injury was studied in the hind legs of dogs. Spherical projectiles were used and velocity and mass were varied. The regional arterial blood flow to the injured thigh was recorded and the energy transfer to the tissues determined. In addition the presence within the aortic arch was recorded immediately after the impact of the missile. Missile penetration caused a marked peak of flow followed by a less pronounced elevation of the flow level for at least 30 minutes. The magnitude of the peak was related to the amount of energy transferred to the tissues. The origin of the circulatory changes is discussed. Shock waves of considerable magnitude were recorded within the aortic arch in connection with the bullet penetration.

Animals↗
PubMed1979

The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer.

The measurement of the efficiency of Förster long-range resonance energy transfer between donor (D) and acceptor (A) luminophores attached to the same macromolecular substrate can be used to estimate the D-A separation, R. If the D and A transition dipoles sample all orientations with respect to the substrate (the isotropic condition) in a time short compared with the transfer time (the dynamic averaging condition), the average orientation factor less than K2 greater than is 2/3. If the isotropic condition is not satisfied but the dynamic averaging condition is, upper and lower bounds for less than K2 greater than, and thus R, may be obtained from observed D and A depolarizations, and these limits may be further narrowed if the transfer depolarization is also known. This paper offers experimental protocols for obtaining this reorientational information and presents contour plots of less than K2 greater than min and less than K2 greater than max as functions of generally observable depolarizations. This permits an uncertainty to be assigned to the determined value of R. The details of the D and A reoreintational process need not be known, but the orientational distributions are assumed to have at least approximate axial symmetry with respect to a stationary substrate. Average depolarization factors are derived for various orientational distribution functions that demonstrate the effects of various mechanisms for reorientation of the luminophores. It is shown that in general the static averaging regime does not lend itself to determinations of R.

Energy Transfer↗
PubMed1979

Fluorescence energy transfer between subfragment-1 and actin points in the rigor complex of actosubfragment-1.

The fast-reacting thiol (SH1) of myosin subfragment-1 (S-1) was covalently and specifically labeled with (iodoacetamido)fluorescein (IAF), while Cys-373 of actin was also covalently and preferentially labeled with N-(iodoacetyl)-N'-(1-sulfo-5-naphthyl)ethylenediamine (1,5-IAEDANS). The method of fluorescence energy transfer was used to examine the spatial proximity between the two sites, i.e., SH1 and Cys-373, in the rigor complex of acto-S-1. Approximately 30% fluorescence energy transfer was observed from the 1,5-IAEDANS on actin as a donor to the IAF on S-1 as an acceptor in their rigor complex; under certain assumptions this corresponds to a distance of ca. 6.0 nm.

Actins↗
PubMedDate not supplied

[Picosecond energy transfer between the spectral forms of pigments from the reaction center of Rhodospirillum rubrum].

Absorption changes of reaction centers from Rhodospirillum rubrum at 748, 796 and 870 nm induced by 532 and 870 nm picosecond light pulses were investigated with a picosecond spectrometer. Kinetics of absorption changes at 748 and 796 had an additional bleaching when induced by the 532 nm pulse, in comparison with those at 870 nm. The additional bleaching was interpreted as a result of the excitation energy transfer via spectral forms of pigments of reaction centers. The experimental results fit the mathematical simulation of the additional bleaching for the following set of rate constant values: intrinsic conversion to the lowest excited singlet state in bacteriopheophytine molecule--10(13) s-1, energy transfer from bacteriopheophytine to P800 3.10(12) s-1, from P800 to P870--2.10(12) s-1.

Chlorophyll↗
PubMed1977

Reconstituted energy transfer from antenna pigment-protein to reaction centres isolated from Rhodopseudomonas sphaeroides.

Efficient energy transfer has been reconstituted between an antenna pigment-protein and reaction centres isolated from the photosynthetic membrane of Rhodopseudomonas sphaeroides. The reconstituted system has fluorescence induction kinetics and fluorescence yields similar to those obtained from antenna bacteriochlorophyll in chromatophores. The results indicated that closed reaction centres quench fluorescence from the antenna pigment-protein, although not as strongly as photochemically active reaction centres. The measurement of fluorescence yields from chromatophores of the reaction centreless mutant PM-8 and of the parent strain Ga confirmed these observations. The fluorescence yield from the reconstituted system was approximately the same whether the reaction centres had been closed by photo-oxidation of the bacteriochlorophyll electron donor or chemical reduction of the primary acceptor, indicating a similar lifetime for the excited singlet state in both states of the reaction centres.

Bacteriochlorophylls↗
PubMed1979

The association between major sialoglycoprotein and spectrin of human erythrocyte membranes as detected by fluorescence resonance energy transfer.

The interactions among the major sialoglycoprotein and peripheral proteins of human erythrocyte membranes were investigated by the long range resonance energy transfer between different fluorescent moieties separately conjugated to proteins. Consequently, direct association between the major sialoglycoprotein and spectrin was observed and divalent cations were required for their association.

Energy Transfer↗
PubMed1978

Topographical analysis of regulatory and metal ion binding sites on glutamine synthetase from Escherichia coli: 13C and 31P nuclear magnetic resonance and fluorescence energy transfer study.

The paramagnetic effect of Mn(II) on (13)C and (31)P nuclear magnetic resonance signals from the [2-(13)C]ATP adenylylated glutamine synthetase [L-glutamate:ammonia ligase (ADP-forming); EC 6.3.1.2] from Escherichia coli was measured. This effect permitted the determination of distances from the 2-C position and the phosphorus of covalently bound AMP to the two Mn(II) binding sites, n(1) and n(2). Binding of Mn(II) to the n(1) site converts an inactive apo-enzyme to its active form, while the metal ion bound at n(2) occupies the metal-nucleotide substrate site. The distances from Mn(II) at the n(1) and n(2) sites to phosphorus are approximately 10 and approximately 7 A and to the 2-C position of the adenine ring are approximately 12 and approximately 11 A, respectively. The fluorescence energy transfer method was used to determine distances between Co(II) at n(1) and n(2) and the adenylyl site. For this experiment the enzyme was adenylylated with epsilon-ATP. The distances between epsilon-adenine and Co(II) at n(1) and n(2) are approximately 13 and approximately 11 A, respectively. Quantitation of the paramagnetic effect due to Co(II) on the (31)P nuclear magnetic resonance signal yielded values of 8 and 6 A for the distances between the phosphorus of the covalently bound AMP and the n(1) and n(2) sites, respectively. The results reveal that the covalent modification site is very close to the catalytic center of the enzyme. In this study both nuclear magnetic resonance and fluorescence energy transfer techniques have been used to determine distances between the same set of sites on an enzyme surface.

Adenosine Monophosphate↗
PubMed1977

Fluorescence energy transfer between heterologous active sites of affinity-labeled aspartokinase of Escherichia coli.

The distance between aspartokinase and homoserine dehydrogenase active sites was determined using fluorescence energy transfer between modified substrates. The fluorescent 1,N(6)-ethenoadenosine 5'-triphosphate was bound at the kinase active site by Co(III) affinity labeling. Reduced thionicotinamide adenine dinucleotide phosphate quenched the fluorescence of bound nucleotide. Fluorescence depolarization measurements led to a delimitation of the value of the dipolar orientation factor to the range 0.3 to 2.8. The distance between the fluorescent probe and the quencher was 29 +/- 4 A. In the presence of threonine, this distance increased to 36 +/- 5 A. Threonine binding either increased the intersite distance by ca. 7 A or caused a reorientation of the probe at the dehydrogenase site.

Affinity Labels↗
PubMed1978

Factors affecting energy transfer from phycobilisomes to thylakoids in Anacystis nidulans.

Short illumination with white light of dark-maintained Anacystis nidulans prior to immersion in liquid nitrogen resulted in a marked change of fluorescence emission characteristics at 77 K. The fluorescence of Photosystem II-associated membrane bound pigments increases, while the emission due to phycobilins decreases. This effect seems to be due to a light-dependent alteration in the extent of contact between phycobilisomes and thylakoids, since the effect is reversible in the dark and is abolished by short glutaraldehyde fixation. The preillumination effect is not inhibited by DCMU. Emission spectra obtained with actively growing and CO2-starved cells indicate that the light-dependent increase in energy transfer from phycobilins to chlorophyll depends upon the physiological state of the cells.

Chlorophyll↗