Coenzyme models. 46. "Remote control" of flavin reactivities by an intramolecular crown ring serving as a metal binding site: Relationship between spectral properties and dissociation of the 8-sulfonamide group

Seiji Shinkai, Kei Kameoka, Kaori Ueda, Osamu Manabe, Masayoshi Onishi

研究成果: ジャーナルへの寄稿記事

5 引用 (Scopus)

抄録

Crown ether flavin mimics (CrSO2NHFl and NCrSO2NHFl) which have a flavin moiety serving as a catalytic site and a crown ether moiety serving as a metal binding site at the two sides of a sulfonamide group were synthesized. We have found that the absorption spectra of these flavins are very sensitive to solvent effects; that is, they are yellow to orange in nonpolar solvents like "regular" flavins but imparted a red color to polar solvents characteristic of the intramolecular charge transfer like roseoflavin. This is due to the dissociation of the 8-sulfonamide group in polar solvents. The fluorescence spectra were also sensitive to solvent effects: the quantum yields of neutral NCrSO2NHFl increased with decreasing solvent polarity. In acetonitrile, Ca2+ ion bound to the crown ether cavity in NCrSO2NHFl facilitated deprotonation of the sulfonamide group to give a new absorption maximum at 452 nm. Correspondingly, the quantum yields for photooxidation of benzyl alcohol by NCrSO2NHFl increased with increasing Ca2+ concentration. These findings indicate that Ca2+ ion can control the catalytic activity of NCrSO2NHFl through the interaction with the sulfonamide group serving as a cap for Ca2+ bound to the crown cavity. The changes in the absorption spectra and the quantum yields were not observed for CrSO2NHFl and a reference flavin, PhSO2NHFl. Therefore, NCrSO2NHFl acts as a new model system relevant to allosteric enzymes in which binding of an effector to a remote, allosteric site induces activity changes in the active sites.

元の言語英語
ページ(範囲)269-282
ページ数14
ジャーナルBioorganic Chemistry
15
発行部数3
DOI
出版物ステータス出版済み - 1 1 1987
外部発表Yes

Fingerprint

Coenzymes
Sulfonamides
Remote control
Crowns
Metals
Binding Sites
Crown Ethers
Quantum yield
Flavins
Absorption spectra
Catalytic Domain
Ions
Allosteric Site
Benzyl Alcohol
Deprotonation
Photooxidation
4,6-dinitro-o-cresol
Charge transfer
Catalyst activity
Color

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Drug Discovery
  • Organic Chemistry

これを引用

Coenzyme models. 46. "Remote control" of flavin reactivities by an intramolecular crown ring serving as a metal binding site : Relationship between spectral properties and dissociation of the 8-sulfonamide group. / Shinkai, Seiji; Kameoka, Kei; Ueda, Kaori; Manabe, Osamu; Onishi, Masayoshi.

:: Bioorganic Chemistry, 巻 15, 番号 3, 01.01.1987, p. 269-282.

研究成果: ジャーナルへの寄稿記事

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abstract = "Crown ether flavin mimics (CrSO2NHFl and NCrSO2NHFl) which have a flavin moiety serving as a catalytic site and a crown ether moiety serving as a metal binding site at the two sides of a sulfonamide group were synthesized. We have found that the absorption spectra of these flavins are very sensitive to solvent effects; that is, they are yellow to orange in nonpolar solvents like {"}regular{"} flavins but imparted a red color to polar solvents characteristic of the intramolecular charge transfer like roseoflavin. This is due to the dissociation of the 8-sulfonamide group in polar solvents. The fluorescence spectra were also sensitive to solvent effects: the quantum yields of neutral NCrSO2NHFl increased with decreasing solvent polarity. In acetonitrile, Ca2+ ion bound to the crown ether cavity in NCrSO2NHFl facilitated deprotonation of the sulfonamide group to give a new absorption maximum at 452 nm. Correspondingly, the quantum yields for photooxidation of benzyl alcohol by NCrSO2NHFl increased with increasing Ca2+ concentration. These findings indicate that Ca2+ ion can control the catalytic activity of NCrSO2NHFl through the interaction with the sulfonamide group serving as a cap for Ca2+ bound to the crown cavity. The changes in the absorption spectra and the quantum yields were not observed for CrSO2NHFl and a reference flavin, PhSO2NHFl. Therefore, NCrSO2NHFl acts as a new model system relevant to allosteric enzymes in which binding of an effector to a remote, allosteric site induces activity changes in the active sites.",
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N2 - Crown ether flavin mimics (CrSO2NHFl and NCrSO2NHFl) which have a flavin moiety serving as a catalytic site and a crown ether moiety serving as a metal binding site at the two sides of a sulfonamide group were synthesized. We have found that the absorption spectra of these flavins are very sensitive to solvent effects; that is, they are yellow to orange in nonpolar solvents like "regular" flavins but imparted a red color to polar solvents characteristic of the intramolecular charge transfer like roseoflavin. This is due to the dissociation of the 8-sulfonamide group in polar solvents. The fluorescence spectra were also sensitive to solvent effects: the quantum yields of neutral NCrSO2NHFl increased with decreasing solvent polarity. In acetonitrile, Ca2+ ion bound to the crown ether cavity in NCrSO2NHFl facilitated deprotonation of the sulfonamide group to give a new absorption maximum at 452 nm. Correspondingly, the quantum yields for photooxidation of benzyl alcohol by NCrSO2NHFl increased with increasing Ca2+ concentration. These findings indicate that Ca2+ ion can control the catalytic activity of NCrSO2NHFl through the interaction with the sulfonamide group serving as a cap for Ca2+ bound to the crown cavity. The changes in the absorption spectra and the quantum yields were not observed for CrSO2NHFl and a reference flavin, PhSO2NHFl. Therefore, NCrSO2NHFl acts as a new model system relevant to allosteric enzymes in which binding of an effector to a remote, allosteric site induces activity changes in the active sites.

AB - Crown ether flavin mimics (CrSO2NHFl and NCrSO2NHFl) which have a flavin moiety serving as a catalytic site and a crown ether moiety serving as a metal binding site at the two sides of a sulfonamide group were synthesized. We have found that the absorption spectra of these flavins are very sensitive to solvent effects; that is, they are yellow to orange in nonpolar solvents like "regular" flavins but imparted a red color to polar solvents characteristic of the intramolecular charge transfer like roseoflavin. This is due to the dissociation of the 8-sulfonamide group in polar solvents. The fluorescence spectra were also sensitive to solvent effects: the quantum yields of neutral NCrSO2NHFl increased with decreasing solvent polarity. In acetonitrile, Ca2+ ion bound to the crown ether cavity in NCrSO2NHFl facilitated deprotonation of the sulfonamide group to give a new absorption maximum at 452 nm. Correspondingly, the quantum yields for photooxidation of benzyl alcohol by NCrSO2NHFl increased with increasing Ca2+ concentration. These findings indicate that Ca2+ ion can control the catalytic activity of NCrSO2NHFl through the interaction with the sulfonamide group serving as a cap for Ca2+ bound to the crown cavity. The changes in the absorption spectra and the quantum yields were not observed for CrSO2NHFl and a reference flavin, PhSO2NHFl. Therefore, NCrSO2NHFl acts as a new model system relevant to allosteric enzymes in which binding of an effector to a remote, allosteric site induces activity changes in the active sites.

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