Literature DB >> 3576185

On the prevalence of room-temperature protein phosphorescence.

J M Vanderkooi, D B Calhoun, S W Englander.   

Abstract

A large number of proteins were tested for the property of intrinsic phosphorescence in deoxygenated aqueous solution at room temperature. The majority of proteins exhibit phosphorescence under normal solution conditions. Phosphorescence lifetimes from 0.5 millisecond to 2 seconds were observed in three-fourths of the proteins tested. The lifetime appears to correlate with relative isolation of the tryptophan indole side chain from solvent. With few exceptions, proteins in general can be expected to display a phosphorescence lifetime greater than 30 microseconds. This widespread characteristic of proteins has been largely overlooked because long-lived phosphorescence is highly sensitive to quenching by low levels of dissolved oxygen in solution. Protein phosphorescence offers a new time domain and a far wider dynamic range than has been used before for photoluminescence experimentation.

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Year:  1987        PMID: 3576185      PMCID: PMC3438914          DOI: 10.1126/science.3576185

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  9 in total

1.  A note on the phosphorescence of proteins.

Authors:  P DEBYE; J O EDWARDS
Journal:  Science       Date:  1952-08-08       Impact factor: 47.728

2.  Room temperature phosphorescence and the dynamic aspects of protein structure.

Authors:  M L Saviotti; W C Galley
Journal:  Proc Natl Acad Sci U S A       Date:  1974-10       Impact factor: 11.205

3.  Measurement and calibration of peptide group hydrogen-deuterium exchange by ultraviolet spectrophotometry.

Authors:  J J Englander; D B Calhoun; S W Englander
Journal:  Anal Biochem       Date:  1979-01-15       Impact factor: 3.365

4.  The amino acid sequence of Pseudomonas fluorescens azurin.

Authors:  R P Ambler; L H Brown
Journal:  Biochem J       Date:  1967-09       Impact factor: 3.857

5.  Singular oxygen effects on the room-temperature phosphorescence of alcohol dehydrogenase from horse liver.

Authors:  G B Strambini
Journal:  Biophys J       Date:  1983-07       Impact factor: 4.033

6.  Phosphorescence of tryptophan from parvalbumin and actin in liquid solution.

Authors:  T Horie; J M Vanderkooi
Journal:  FEBS Lett       Date:  1982-10-04       Impact factor: 4.124

7.  Protein fluorescence quenching by small molecules: protein penetration versus solvent exposure.

Authors:  D B Calhoun; J M Vanderkooi; G R Holtom; S W Englander
Journal:  Proteins       Date:  1986-10

8.  Flash photolysis of human serum albumin: characterization of the indole triplet absorption spectrum and decay at ambient temperature.

Authors:  B Hicks; M White; C A Ghiron; R R Kuntz; W A Volkert
Journal:  Proc Natl Acad Sci U S A       Date:  1978-03       Impact factor: 11.205

9.  Penetration of dioxygen into proteins studied by quenching of phosphorescence and fluorescence.

Authors:  D B Calhoun; J M Vanderkooi; G V Woodrow; S W Englander
Journal:  Biochemistry       Date:  1983-03-29       Impact factor: 3.162

  9 in total
  15 in total

1.  Effect of heavy water on protein flexibility.

Authors:  Patrizia Cioni; Giovanni B Strambini
Journal:  Biophys J       Date:  2002-06       Impact factor: 4.033

2.  Time-resolved circularly polarized protein phosphorescence.

Authors:  J A Schauerte; D G Steel; A Gafni
Journal:  Proc Natl Acad Sci U S A       Date:  1992-11-01       Impact factor: 11.205

Review 3.  Emerging applications of phosphorescent metalloporphyrins.

Authors:  Dmitri B Papkovsky; Tomás C O'Riordan
Journal:  J Fluoresc       Date:  2005-07       Impact factor: 2.217

4.  Detection of a pH-dependent conformational change in azurin by time-resolved phosphorescence.

Authors:  J E Hansen; D G Steel; A Gafni
Journal:  Biophys J       Date:  1996-10       Impact factor: 4.033

5.  Role of domain interactions in the collective motion of phosphoglycerate kinase.

Authors:  Gusztáv Schay; Levente Herényi; Judit Fidy; Szabolcs Osváth
Journal:  Biophys J       Date:  2013-02-05       Impact factor: 4.033

6.  Evidence for ligand-induced conformational changes in proteins from phosphorescence spectroscopy.

Authors:  Z Li; W C Galley
Journal:  Biophys J       Date:  1989-08       Impact factor: 4.033

7.  In vitro renaturation of bovine beta-lactoglobulin A leads to a biologically active but incompletely refolded state.

Authors:  V Subramaniam; D G Steel; A Gafni
Journal:  Protein Sci       Date:  1996-10       Impact factor: 6.725

8.  Excited states of tryptophan in cod parvalbumin. Identification of a short-lived emitting triplet state at room temperature.

Authors:  K Sudhakar; C M Phillips; S A Williams; J M Vanderkooi
Journal:  Biophys J       Date:  1993-05       Impact factor: 4.033

9.  Reactions of excited triplet states of metal substituted myoglobin with dioxygen and quinone.

Authors:  S Papp; J M Vanderkooi; C S Owen; G R Holtom; C M Phillips
Journal:  Biophys J       Date:  1990-07       Impact factor: 4.033

10.  Long-range electron exchange measured in proteins by quenching of tryptophan phosphorescence.

Authors:  J M Vanderkooi; S W Englander; S Papp; W W Wright; C S Owen
Journal:  Proc Natl Acad Sci U S A       Date:  1990-07       Impact factor: 11.205

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