Binding of acridine orange to transfer RNA and photodynamic inactivation.

The kinetics of the photodynamic desactivation of lysozyme in presence of acridine orange as the sensitizer have been investigated in detail varying oxygen, protein, dye concentration, ionic strength and pH value. The kinetics can be approximately described as an over all pseudo-first- order rate process. Changing the solvent from water to D2O or by quenching experiments in presence of azide ions it could be shown that the desactivation of lysozyme is caused exclusively by singlet oxygen. The excited oxygen occurs via the triplet state of the dye with a rate constant considerably lower than that to be expected for a diffusionally controlled reaction. Singlet oxygen reacts chemically (desactivation, k=2.9 × 107 ᴍ-1 sec-1) and physically (quenching process, k = 4.1 × 108 ᴍ-1sec-1) with the enzyme. The kinetical analysis shows that additional chemical reactions between singlet oxygen and lysozyme would have only little influence on the kinetics of the desactivation as long as their products would be enzymatically active and their kinetical constants would be less than about 1 × 108 ᴍ-1 sec-1.

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The photodynamic inactivation of tobacco mosaic virus and its ribonucleic acid by acridine orange

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis ◽

10.1016/0005-2787(66)90005-0 ◽

1966 ◽

Vol 129 (1) ◽

pp. 32-41 ◽

Cited By ~ 43

Author(s):

K.Sivarama Sastry ◽

Milton P. Gordon

Keyword(s):

Tobacco Mosaic Virus ◽

Acridine Orange ◽

Mosaic Virus ◽

Ribonucleic Acid ◽

Photodynamic Inactivation

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Photodynamic Inactivation with Acridine Orange on a Multidrug-resistant Mouse Osteosarcoma Cell Line

Japanese Journal of Cancer Research ◽

10.1111/j.1349-7006.2000.tb00964.x ◽

2000 ◽

Vol 91 (4) ◽

pp. 439-445 ◽

Cited By ~ 29

Author(s):

Katsuyuki Kusuzaki ◽

Ginjirou Minami ◽

Hideyuki Takeshita ◽

Hiroaki Murata ◽

Shin Hashiguchi ◽

...

Keyword(s):

Acridine Orange ◽

Cell Line ◽

Multidrug Resistant ◽

Osteosarcoma Cell Line ◽

Osteosarcoma Cell ◽

Photodynamic Inactivation ◽

Resistant Mouse

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Induced circular dichroism of acridine orange bound to double-stranded RNA and transfer RNA

Biopolymers ◽

10.1002/bip.1976.360150907 ◽

1976 ◽

Vol 15 (9) ◽

pp. 1693-1699 ◽

Cited By ~ 11

Author(s):

Mitsuo Zama ◽

Sachiko Ichimura

Keyword(s):

Circular Dichroism ◽

Acridine Orange ◽

Transfer Rna ◽

Induced Circular Dichroism ◽

Double Stranded Rna ◽

Circular Dichroïsm

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Polarized fluorescence of acridine orange-transfer RNA complexes

FEBS Letters ◽

10.1016/0014-5793(70)80263-0 ◽

1970 ◽

Vol 8 (4) ◽

pp. 201-204 ◽

Cited By ~ 8

Author(s):

A. Surovaya ◽

O. Borisova ◽

T. Jilyaeva ◽

V. Scheinker ◽

L. Kisselev

Keyword(s):

Acridine Orange ◽

Transfer Rna ◽

Polarized Fluorescence ◽

Rna Complexes

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On the Mechanism of the Acridine Orange Sensitized Photodynamic Inactivation of Lysozyme II. Kinetics in Presence of N-Acetylglucosamine

Zeitschrift für Naturforschung C ◽

10.1515/znc-1976-11-1209 ◽

1976 ◽

Vol 31 (11-12) ◽

pp. 679-682 ◽

Cited By ~ 3

Author(s):

Peter Rosenkranz ◽

Hartmut Schmidt

Keyword(s):

Amino Acid ◽

Triplet State ◽

Singlet Oxygen ◽

Acridine Orange ◽

Rate Constant ◽

Enzymatic Reaction ◽

Photodynamic Inactivation ◽

Tryptophan Residues ◽

Amino Acid Side Chains ◽

Kinetics Of

Abstract The photodynamic deactivation of lysozyme in presence of acridine orange is caused by a reaction between singlet oxygen formed via the dye triplet state and the protein. In order to identify the region where the singlet oxygen reacts with the protein we have investigated the kinetics of the deactivation in presence of the inhibitor of the enzymatic reaction N-acetylglucosamine (GlcNAc). The overall experimental rate constant becomes slower with increasing saccharide concentrations. As we can exclude experimentally that this kinetical effect is caused in presence of the saccharide by a physical quenching of singlet oxygen or of the dye triplet state it has to be assumed that GlcNAc protects the surrounding of its binding place at subsite C of the enzymatic center sterically against an attack of singlet oxygen. In this region three tryptophan residues are located, which could be sensitive against singlet oxygen. Surprisingly, however, it has been found that only those species are protected, in which a second saccharide molecule is bound to the protein, probably at subsite E at the enzymatic center, where no sensitive amino acid side chains are located.

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