Dataset Information

Fluorescence Quenching-Based Mechanism for Determination of Hypochlorite by Coumarin-Derived Sensors.

ABSTRACT: A fluorescence quenching-based mechanism for the determination of hypochlorite was proposed based on spectroscopic and chromatographic studies on the hypochlorite-sensing potency of three structurally similar and highly fluorescent coumarins. The mode of action was found to rely upon a chlorination of the coumarin-based probes resulting from their reaction with sodium hypochlorite. Importantly, the formation of chlorinated derivatives was accompanied by a linear decrease in the fluorescence intensities of the probes tested. The results obtained suggest the applicability of a coumarin-dependent hypochlorite recognition mechanism for the detection of, as well as for quantitative determination of, hypochlorite species in vitro.

SUBMITTER: Starzak K

PROVIDER: S-EPMC6358793 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature

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Fluorescence Quenching-Based Mechanism for Determination of Hypochlorite by Coumarin-Derived Sensors.

Starzak Karolina K Matwijczuk Arkadiusz A Creaven Bernadette B Matwijczuk Alicja A Wybraniec Sławomir S Karcz Dariusz D

International journal of molecular sciences 20190111 2

A fluorescence quenching-based mechanism for the determination of hypochlorite was proposed based on spectroscopic and chromatographic studies on the hypochlorite-sensing potency of three structurally similar and highly fluorescent coumarins. The mode of action was found to rely upon a chlorination of the coumarin-based probes resulting from their reaction with sodium hypochlorite. Importantly, the formation of chlorinated derivatives was accompanied by a linear decrease in the fluorescence inte ...[more]

PMID: 30642004

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Project description:Human gammaD-crystallin (HgammaD-Crys) is a two-domain, beta-sheet eye lens protein found in the lens nucleus. Its long-term solubility and stability are important to maintain lens transparency throughout life. HgammaD-Crys has four highly conserved buried tryptophans (Trps), with two in each of the homologous beta-sheet domains. In situ, these Trps will be absorbing ambient UV radiation that reaches the lens. The dispersal of the excited-state energy to avoid covalent damage is likely to be physiologically relevant for the lens crystallins. Trp fluorescence is efficiently quenched in native HgammaD-Crys. Previous steady-state fluorescence measurements provide strong evidence for energy transfer from Trp42 to Trp68 in the N-terminal domain and from Trp130 to Trp156 in the C-terminal domain [Chen, J., et al. (2006) Biochemistry 45, 11552-11563]. Hybrid quantum mechanical-molecular mechanical (QM-MM) simulations indicated that the fluorescence of Trp68 and Trp156 is quenched by fast electron transfer to the amide backbone. Here we report additional information obtained using time-resolved fluorescence spectroscopy. In the single-Trp-containing proteins (Trp42-only, Trp68-only, Trp130-only, and Trp156-only), the highly quenched Trp68 and Trp156 have very short lifetimes, tau approximately 0.1 ns, whereas the moderately fluorescent Trp42 and Trp130 have longer lifetimes, tau approximately 3 ns. In the presence of the energy acceptor (Trp68 or Trp156), the lifetime of the energy donor (Trp42 or Trp130) decreased from approximately 3 to approximately 1 ns. The intradomain energy transfer efficiency is 56% in the N-terminal domain and is 71% in the C-terminal domain. The experimental values of energy transfer efficiency are in good agreement with those calculated theoretically. The absence of a time-dependent red shift in the time-resolved emission spectra of Trp130 proves that its local environment is very rigid. Time-resolved fluorescence anisotropy measurements with the single-Trp-containing proteins, Trp42-only and Trp130-only, indicate that the protein rotates as a rigid body and no segmental motion is detected. A combination of energy transfer with electron transfer results in short excited-state lifetimes of all Trps, which, together with the high rigidity of the protein matrix around Trps, could protect HgammaD-Crys from excited-state reactions causing permanent covalent damage.

Dataset Information

Fluorescence Quenching-Based Mechanism for Determination of Hypochlorite by Coumarin-Derived Sensors.

Publications

Fluorescence Quenching-Based Mechanism for Determination of Hypochlorite by Coumarin-Derived Sensors.

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