Literature DB >> 2096899

Dynamic fluorescence in copper proteins. Selected examples.

N Rosato1, E Gratton, G Mei, I Savini, A Finazzi Agrò.   

Abstract

The fluorescence properties of three copper proteins, namely human superoxide dismutase, Pseudomonas aeruginosa azurin and Thiobacillus versutus amicyanin have been studied. All these proteins show a non-exponential decay of fluorescence, though the tryptophanyl residues responsible for the emission are very differently located in the three proteins. All the three decays can be fitted by at least two lifetimes or better with one or two lorentzian-shaped, continuous distributions of lifetime. In each case the removal of copper affects the quantum yield of fluorescence without affecting the shape of the emission.

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Year:  1990        PMID: 2096899     DOI: 10.1007/bf01179522

Source DB:  PubMed          Journal:  Biol Met        ISSN: 0933-5854


  15 in total

1.  Fluorescence lifetime distributions in proteins.

Authors:  J R Alcala; E Gratton; F G Prendergast
Journal:  Biophys J       Date:  1987-04       Impact factor: 4.033

2.  Resolvability of fluorescence lifetime distributions using phase fluorometry.

Authors:  J R Alcala; E Gratton; F G Prendergast
Journal:  Biophys J       Date:  1987-04       Impact factor: 4.033

3.  Environment of copper in Pseudomonas fluorescens azurin: fluorometric approach.

Authors:  A Finazzi-Agrò; G Rotilio; L Avigliano; P Guerrieri; V Boffi; B Mondovì
Journal:  Biochemistry       Date:  1970-04-28       Impact factor: 3.162

Review 4.  Time-resolved fluorescence of proteins.

Authors:  J M Beechem; L Brand
Journal:  Annu Rev Biochem       Date:  1985       Impact factor: 23.643

5.  Subnanosecond motions of tryptophan residues in proteins.

Authors:  I Munro; I Pecht; L Stryer
Journal:  Proc Natl Acad Sci U S A       Date:  1979-01       Impact factor: 11.205

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

Authors:  D Barra; F Martini; J V Bannister; M E Schininà; G Rotilio; W H Bannister; F Bossa
Journal:  FEBS Lett       Date:  1980-10-20       Impact factor: 4.124

7.  Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase.

Authors:  J A Tainer; E D Getzoff; K M Beem; J S Richardson; D C Richardson
Journal:  J Mol Biol       Date:  1982-09-15       Impact factor: 5.469

8.  A time-resolved fluorescence study of human copper-zinc superoxide dismutase.

Authors:  N Rosato; G Mei; E Gratton; J V Bannister; W H Bannister; A Finazzi-Agrò
Journal:  Biophys Chem       Date:  1990-05       Impact factor: 2.352

9.  Confirmation that multiexponential fluorescence decay behavior of holoazurin originates from conformational heterogeneity.

Authors:  C M Hutnik; A G Szabo
Journal:  Biochemistry       Date:  1989-05-02       Impact factor: 3.162

10.  Conformational heterogeneity of the copper binding site in azurin. A time-resolved fluorescence study.

Authors:  A G Szabo; T M Stepanik; D M Wayner; N M Young
Journal:  Biophys J       Date:  1983-03       Impact factor: 4.033

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  1 in total

1.  Origin of tryptophan fluorescence lifetimes. Part 2: fluorescence lifetimes origin of tryptophan in proteins.

Authors:  J R Albani
Journal:  J Fluoresc       Date:  2013-08-03       Impact factor: 2.217

  1 in total

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