Model Systems for Flavoenzyme Activity: Relationships between Cofactor Structure, Binding and Redox Properties

Yves Marie Legrand; Mark Gray; Graeme Cooke; Vincent M. Rotello

doi:10.1021/ja036940b

Model Systems for Flavoenzyme Activity: Relationships between Cofactor Structure, Binding and Redox Properties

Yves Marie Legrand, Mark Gray, Graeme Cooke, Vincent M. Rotello

School of Engineering & Physical Sciences

Research output: Contribution to journal › Article › peer-review

71 Citations (Scopus)

Abstract

A series of flavins were synthesized bearing electron-withdrawing and -donating substituents. The electrochemical properties of these flavins in a nonpolar solvent were determined. The recognition of these flavins by a diamidopyridine (DAP) receptor and the effect this receptor has on flavin redox potential was also quantified. It was found that the DAP-flavin binding affinity and the reduction potentials (E_1/2) for both the DAP-bound and unbound flavins correlated well with functions derived from linear free energy relationships (LFERs). These results provide insight and predictive capability for the interplay of electronics and redox state-specific interactions for both abiotic and enzymatic systems.

Original language	English
Pages (from-to)	15789-15795
Number of pages	7
Journal	Journal of the American Chemical Society
Volume	125
Issue number	51
DOIs	https://doi.org/10.1021/ja036940b
Publication status	Published - 24 Dec 2003

Access to Document

10.1021/ja036940b

Cite this

@article{8c359bafbe4f4f8480ed4384a819f388,

title = "Model Systems for Flavoenzyme Activity: Relationships between Cofactor Structure, Binding and Redox Properties",

abstract = "A series of flavins were synthesized bearing electron-withdrawing and -donating substituents. The electrochemical properties of these flavins in a nonpolar solvent were determined. The recognition of these flavins by a diamidopyridine (DAP) receptor and the effect this receptor has on flavin redox potential was also quantified. It was found that the DAP-flavin binding affinity and the reduction potentials (E1/2) for both the DAP-bound and unbound flavins correlated well with functions derived from linear free energy relationships (LFERs). These results provide insight and predictive capability for the interplay of electronics and redox state-specific interactions for both abiotic and enzymatic systems.",

author = "Legrand, {Yves Marie} and Mark Gray and Graeme Cooke and Rotello, {Vincent M.}",

year = "2003",

month = dec,

day = "24",

doi = "10.1021/ja036940b",

language = "English",

volume = "125",

pages = "15789--15795",

journal = "Journal of the American Chemical Society",

issn = "1520-5126",

publisher = "American Chemical Society",

number = "51",

}

TY - JOUR

T1 - Model Systems for Flavoenzyme Activity

T2 - Relationships between Cofactor Structure, Binding and Redox Properties

AU - Legrand, Yves Marie

AU - Gray, Mark

AU - Cooke, Graeme

AU - Rotello, Vincent M.

PY - 2003/12/24

Y1 - 2003/12/24

N2 - A series of flavins were synthesized bearing electron-withdrawing and -donating substituents. The electrochemical properties of these flavins in a nonpolar solvent were determined. The recognition of these flavins by a diamidopyridine (DAP) receptor and the effect this receptor has on flavin redox potential was also quantified. It was found that the DAP-flavin binding affinity and the reduction potentials (E1/2) for both the DAP-bound and unbound flavins correlated well with functions derived from linear free energy relationships (LFERs). These results provide insight and predictive capability for the interplay of electronics and redox state-specific interactions for both abiotic and enzymatic systems.

AB - A series of flavins were synthesized bearing electron-withdrawing and -donating substituents. The electrochemical properties of these flavins in a nonpolar solvent were determined. The recognition of these flavins by a diamidopyridine (DAP) receptor and the effect this receptor has on flavin redox potential was also quantified. It was found that the DAP-flavin binding affinity and the reduction potentials (E1/2) for both the DAP-bound and unbound flavins correlated well with functions derived from linear free energy relationships (LFERs). These results provide insight and predictive capability for the interplay of electronics and redox state-specific interactions for both abiotic and enzymatic systems.

U2 - 10.1021/ja036940b

DO - 10.1021/ja036940b

M3 - Article

C2 - 14677969

SN - 1520-5126

VL - 125

SP - 15789

EP - 15795

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 51

ER -

Model Systems for Flavoenzyme Activity: Relationships between Cofactor Structure, Binding and Redox Properties

Abstract

Access to Document

Fingerprint

Cite this