Literature DB >> 6349707

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

G B Strambini.   

Abstract

The room-temperature phosphorescence of alcohol dehydrogenase from horse liver in the presence of oxygen has the characteristics of a light-induced emission as it appears only after a certain amount of excitation has been absorbed. The initial lag period, the steady-state intensity, and the duration of the induced state are dominated by the oxygen content of the solution, the rate of light absorption, and the radiation dose. The phenomenon is not unique to this enzyme and the data are consistent with photochemical depletion of oxygen.

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Year:  1983        PMID: 6349707      PMCID: PMC1329276          DOI: 10.1016/S0006-3495(83)84331-8

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


  3 in total

1.  Excited state chemistry of aromatic amino acids and related peptides. III. Tryptophan.

Authors:  D V Bent; E Hayon
Journal:  J Am Chem Soc       Date:  1975-05-14       Impact factor: 15.419

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.  Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale.

Authors:  J R Lakowicz; G Weber
Journal:  Biochemistry       Date:  1973-10-09       Impact factor: 3.162

  3 in total
  8 in total

1.  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

2.  On the prevalence of room-temperature protein phosphorescence.

Authors:  J M Vanderkooi; D B Calhoun; S W Englander
Journal:  Science       Date:  1987-05-01       Impact factor: 47.728

3.  Relevance of divalent cations to ATP-driven proton pumping in beef heart mitochondrial F0F1-ATPase.

Authors:  S Papageorgiou; A B Melandri; G Solaini
Journal:  J Bioenerg Biomembr       Date:  1998-12       Impact factor: 2.945

4.  Modification of the mitochondrial F1-ATPase epsilon subunit, enhancement of the ATPase activity of the IF1-F1 complex and IF1-binding dependence of the conformation of the epsilon subunit.

Authors:  G Solaini; A Baracca; E Gabellieri; G Lenaz
Journal:  Biochem J       Date:  1997-10-15       Impact factor: 3.857

5.  Glycerol effects on protein flexibility: a tryptophan phosphorescence study.

Authors:  M Gonnelli; G B Strambini
Journal:  Biophys J       Date:  1993-07       Impact factor: 4.033

6.  Quenching of alkaline phosphatase phosphorescence by O2 and NO. Evidence for inflexible regions of protein structure.

Authors:  G B Strambini
Journal:  Biophys J       Date:  1987-07       Impact factor: 4.033

7.  Time-resolved room temperature protein phosphorescence: nonexponential decay from single emitting tryptophans.

Authors:  B D Schlyer; J A Schauerte; D G Steel; A Gafni
Journal:  Biophys J       Date:  1994-09       Impact factor: 4.033

8.  Tryptophan phosphorescence of ribonuclease T1 as a probe of protein flexibility.

Authors:  M Gonnelli; A Puntoni; G B Strambini
Journal:  J Fluoresc       Date:  1992-09       Impact factor: 2.217

  8 in total

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