A deuterium isotope solvent effect on fluorescence

Förster, Th.; Rokos, Katharina

doi:10.1016/0009-2614(67)80019-8

Cited by 41 publications

(14 citation statements)

References 9 publications

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“…Literature values of the quantum yield of ANS in H20 are 0.003 (Robinson et al, 1978;Foerster and Rokos, 1967), similar to our value of 0.0025. The apparently anomalous long radiative lifetime of ANS in water (108 ns versus 42 ns, from Eq.…”

Section: Comparisons Based On Fluorescence Spectroscopysupporting

confidence: 90%

Characterization of the sources of protein-ligand affinity: 1-sulfonato-8-(1')anilinonaphthalene binding to intestinal fatty acid binding protein

Kirk

Kurian

Prendergast

1996

Biophysical Journal

114

108

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1-Sulfonato-8-(1')anilinonaphthalene (1,8-ANS) was employed as a fluorescent probe of the fatty acid binding site of recombinant rat intestinal fatty acid binding protein (1-FABP). The enhancement of fluorescence upon binding allowed direct determination of binding affinity by fluorescence titration experiments, and measurement of the effects on that affinity of temperature, pH, and ionic strength. Solvent isotope effects were also determined. These data were compared to results from isothermal titration calorimetry. We obtained values for the enthalpy and entropy of this interaction at a variety of temperatures, and hence determined the change in heat capacity of the system consequent upon binding. The ANS-1-FABP is enthalpically driven; above approximately 14 degrees C it is entropically opposed, but below this temperature the entropy makes a positive contribution to the binding. The changes we observe in both enthalpy and entropy of binding with temperature can be derived from the change in heat capacity upon binding by integration, which demonstrates the internal consistency of our results. Bound ANS is displaced by fatty acids and can itself displace fatty acids bound to I-FABP. The binding site for ANS appears to be inside the solvent-containing cavity observed in the x-ray crystal structure, the same cavity occupied by fatty acid. From the fluorescence spectrum and from an inversion of the Debye-Hueckel formula for the activity coefficients as a function of added salt, we inferred that this cavity is fairly polar in character, which is in keeping with inferences drawn from the x-ray structure. The binding affinity of ANS is considered to be a consequence of both electrostatic and conditional hydrophobic effects. We speculate that the observed change in heat capacity is produced mainly by the displacement of strongly hydrogen-bonded waters from the protein cavity.

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Section: Comparisons Based On Fluorescence Spectroscopysupporting

confidence: 90%

Characterization of the sources of protein-ligand affinity: 1-sulfonato-8-(1')anilinonaphthalene binding to intestinal fatty acid binding protein

Kirk

Kurian

Prendergast

1996

Biophysical Journal

114

108

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“…S7A). In another experiment, we used isotopic substitution of deuterium oxide (D 2 O) for water because D 2 O decreases dynamic quenching of fluorophores . As predicted, the steady‐state fluorescence intensity of NMM in D 2 O increased relative to that in H 2 O (Fig.…”

Section: Resultsmentioning

confidence: 78%

N‐methylmesoporphyrin IX fluorescence as a reporter of strand orientation in guanine quadruplexes

et al. 2014

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Guanine quadruplexes (GQ) are four‐stranded DNA structures formed by guanine‐rich DNA sequences. The formation of GQs inhibits cancer cell growth, although the detection of GQs in vivo has proven difficult, in part because of their structural diversity. The development of GQ‐selective fluorescent reporters would enhance our ability to quantify the number and location of GQs, ultimately advancing biological studies of quadruplex relevance and function. N‐methylmesoporphyrin IX (NMM) interacts selectively with parallel‐stranded GQs; in addition, its fluorescence is sensitive to the presence of DNA, making this ligand a possible candidate for a quadruplex probe. In the present study, we investigated the effect of DNA secondary structure on NMM fluorescence. We found that NMM fluorescence increases by about 60‐fold in the presence of parallel‐stranded GQs and by about 40‐fold in the presence of hybrid GQs. Antiparallel GQs lead to lower than 10‐fold increases in NMM fluorescence. Single‐stranded DNA, duplex, or i‐motif, induce no change in NMM fluorescence. We conclude that NMM shows promise as a ‘turn‐on’ fluorescent probe for detecting quadruplex structures, as well as for differentiating them on the basis of strand orientation.

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“…An alternative explanation, which has been attributed to fluorescence quenching of various organic, inorganic, and nanoparticle fluorophores, is that of excited state relaxation induced by intermolecular hydrogen‐bond formation or proton transfer. Such quenching mechanisms can exhibit strong isotope effects; fluorescence quenching through O–H bonds is much more efficient than through O–D bonds.…”

mentioning

confidence: 99%

The Influence of Water on the Optical Properties of Single‐Layer Molybdenum Disulfide

et al. 2015

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A deuterium isotope solvent effect on fluorescence

Cited by 41 publications

References 9 publications

Characterization of the sources of protein-ligand affinity: 1-sulfonato-8-(1')anilinonaphthalene binding to intestinal fatty acid binding protein

Characterization of the sources of protein-ligand affinity: 1-sulfonato-8-(1')anilinonaphthalene binding to intestinal fatty acid binding protein

N‐methylmesoporphyrin IX fluorescence as a reporter of strand orientation in guanine quadruplexes

The Influence of Water on the Optical Properties of Single‐Layer Molybdenum Disulfide

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