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Title: Effects of pressure upon the fluorescence of the riboflavin binding protein and its flavin mononucleotide complex

Abstract

The effect of pressure in the range of 10/sup -3/-10 kbars upon the ultraviolet fluorescence of the riboflavin binding protein and the fluorescence of its complex with flavin mononucleotide has been studied. The fluorescence spectrum of the isolated protein showed a reversible red shift of 12 nm (1000 cm/sup -1/) at high pressure, indicating the reversible exposure of the tryptophan to solvent. From the pressure dependence of the visible fluorescence of the protein-flavin complex in the region of 1-4 kbars the volume change in dissociation of the protein-ligand complex was estimated to be +3.3 ml/mol. A very sharp increase in fluorescence--up to 30-fold of the low-pressure value--takes place in the region 5-8 kbars. This increase is due to release of the flavin from the complex and is assigned to pressure denaturation of the protein. The midpoint, p/sub /sup 1///sub 2//, of this transition was found at 6.5 kbars and the change in volume, ..delta..V, in the reaction (native-to-denatured) was calculated to be -74 ml/mol. Addition of up to 30 percent methanol results in a progressive decrease both in ..delta..V and p/sub /sup 1///sub 2//, in agreement with the concept that hydrophobic bonding stabilizes the native structure.

Authors:
; ; ;
Publication Date:
Research Org.:
Univ. of Illinois, Urbana
OSTI Identifier:
7156202
Resource Type:
Journal Article
Journal Name:
Biochemistry; (United States)
Additional Journal Information:
Journal Volume: 15:15
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; FLUORESCENCE; PRESSURE DEPENDENCE; PROTEINS; BONDING; RIBOFLAVIN; BIOCHEMISTRY; ISOALLOXAZINES; NUCLEOTIDES; TRYPTOPHAN; AMINO ACIDS; AZOLES; CARBOXYLIC ACIDS; CHEMISTRY; FABRICATION; HETEROCYCLIC ACIDS; HETEROCYCLIC COMPOUNDS; INDOLES; JOINING; LUMINESCENCE; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; ORGANIC OXYGEN COMPOUNDS; PYRROLES; VITAMIN B GROUP; VITAMINS; 550200* - Biochemistry

Citation Formats

Li, T M, Hook, III, J W, Drickamer, H G, and Weber, G. Effects of pressure upon the fluorescence of the riboflavin binding protein and its flavin mononucleotide complex. United States: N. p., 1976. Web. doi:10.1021/bi00660a008.
Li, T M, Hook, III, J W, Drickamer, H G, & Weber, G. Effects of pressure upon the fluorescence of the riboflavin binding protein and its flavin mononucleotide complex. United States. doi:10.1021/bi00660a008.
Li, T M, Hook, III, J W, Drickamer, H G, and Weber, G. Tue . "Effects of pressure upon the fluorescence of the riboflavin binding protein and its flavin mononucleotide complex". United States. doi:10.1021/bi00660a008.
@article{osti_7156202,
title = {Effects of pressure upon the fluorescence of the riboflavin binding protein and its flavin mononucleotide complex},
author = {Li, T M and Hook, III, J W and Drickamer, H G and Weber, G},
abstractNote = {The effect of pressure in the range of 10/sup -3/-10 kbars upon the ultraviolet fluorescence of the riboflavin binding protein and the fluorescence of its complex with flavin mononucleotide has been studied. The fluorescence spectrum of the isolated protein showed a reversible red shift of 12 nm (1000 cm/sup -1/) at high pressure, indicating the reversible exposure of the tryptophan to solvent. From the pressure dependence of the visible fluorescence of the protein-flavin complex in the region of 1-4 kbars the volume change in dissociation of the protein-ligand complex was estimated to be +3.3 ml/mol. A very sharp increase in fluorescence--up to 30-fold of the low-pressure value--takes place in the region 5-8 kbars. This increase is due to release of the flavin from the complex and is assigned to pressure denaturation of the protein. The midpoint, p/sub /sup 1///sub 2//, of this transition was found at 6.5 kbars and the change in volume, ..delta..V, in the reaction (native-to-denatured) was calculated to be -74 ml/mol. Addition of up to 30 percent methanol results in a progressive decrease both in ..delta..V and p/sub /sup 1///sub 2//, in agreement with the concept that hydrophobic bonding stabilizes the native structure.},
doi = {10.1021/bi00660a008},
journal = {Biochemistry; (United States)},
number = ,
volume = 15:15,
place = {United States},
year = {1976},
month = {7}
}