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Literature DB >> 2248991

Fluorescence lifetime distributions in human superoxide dismutase. Effect of temperature and denaturation.

N Rosato¹, E Gratton, G Mei, A Finazzi-Agrò.

Abstract

The internal dynamics of human superoxide dismutase has been studied using time-resolved fluorescence. The fluorescence decay has been analyzed using continuous distribution of lifetime values. The effect of temperature and conformational state on the lifetime distribution has been investigated. The emission of the single tryptophan residue depends on the nature and dynamics of the protein matrix. Conformational changes have been induced by increased concentration of guanidinium hydrochloride. We found that both temperature and conformation strongly effect the width of the lifetime distribution.

Entities: Chemical Species

Mesh：

Substances：
Superoxide Dismutase

Year: 1990 PMID： 2248991 PMCID： PMC1281028 DOI： 10.1016/S0006-3495(90)82427-9

Source DB: PubMed Journal: Biophys J ISSN： 0006-3495 Impact factor: 4.033

15 in total

4. Conformational dynamics of bovine Cu, Zn superoxide dismutase revealed by time-resolved fluorescence spectroscopy of the single tyrosine residue.

Authors: S T Ferreira; L Stella; E Gratton
Journal: Biophys J Date: 1994-04 Impact factor: 4.033

5. Similarity of fluorescence lifetime distributions for single tryptophan proteins in the random coil state.

Authors: R Swaminathan; G Krishnamoorthy; N Periasamy
Journal: Biophys J Date: 1994-11 Impact factor: 4.033

6. Fluorescence study of Escherichia coli cyclic AMP receptor protein.

Authors: M Wasylewski; J Małecki; Z Wasylewski
Journal: J Protein Chem Date: 1995-07

6 in total

Fluorescence lifetime distributions in human superoxide dismutase. Effect of temperature and denaturation.

1. Rotational Brownian motion and polarization of the fluorescence of solutions.

2. Resolvability of fluorescence lifetime distributions using phase fluorometry.

Review 3. Time-resolved fluorescence of proteins.

4. A continuously variable frequency cross-correlation phase fluorometer with picosecond resolution.

Review 5. Multifrequency phase and modulation fluorometry.

6. The fine structure of luminescence spectra of azurin.

7. The complete amino acid sequence of human Cu/Zn superoxide dismutase.

8. Relationship of thermal quenching of protein fluorescence to intramolecular structural mobility.

Review 9. Guanidine hydrochloride denaturation studies of mutant forms of staphylococcal nuclease.

10. Structure and mechanism of copper, zinc superoxide dismutase.

1. Applications of phasor plots to in vitro protein studies.

2. Tryptophan rotamer distributions in amphipathic peptides at a lipid surface.

3. Formation and movement of Fe(III) in horse spleen, H- and L-recombinant ferritins. A fluorescence study.

4. Conformational dynamics of bovine Cu, Zn superoxide dismutase revealed by time-resolved fluorescence spectroscopy of the single tyrosine residue.

5. Similarity of fluorescence lifetime distributions for single tryptophan proteins in the random coil state.

6. Fluorescence study of Escherichia coli cyclic AMP receptor protein.