Substrate binding modulates the reduction potential of DNA photolyase

被引：35

作者：

Gindt, YM ^{[1
]}

Schelvis, JPM

Thoren, KL

Huang, TH

机构：

[1] Lafayette Coll, Dept Chem, Easton, PA 18042 USA

[2] NYU, Dept Chem, New York, NY 10003 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2005年 / 127卷 / 30期

关键词：

D O I：

10.1021/ja051441r

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The reduction potential of the (FADH-/FADH•) couple in DNA photolyase was measured, and the value was found to be significantly higher than the values estimated in the literature. In the absence of substrate, the enzyme has a reduction potential of 16 ± 6 mV vs NHE. In the presence of excess substrate the reduction potential increases to 81 ± 8 mV vs NHE. The increase in reduction potential has physiological relevance since it gives the catalytic state greater resistance to oxidation. This is the first measurement of a reduction potential for this class of DNA-repair enzymes and the larger family of blue-light photoreceptors. Copyright © 2005 American Chemical Society.

引用

收藏

页码：10472 / 10473

页数：2

相关论文

共 42 条

[1] Theoretical study of electron transfer between the photolyase catalytic cofactor FADH- and DNA thymine dimer [J].

Antony, J ;

Medvedev, DM ;

Stuchebrukhov, AA .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2000, 122 (06) :1057-1065

[2] Intraprotein radical transfer during photoactivation of DNA photolyase [J].

Aubert, C ;

Vos, MH ;

Mathis, P ;

Eker, APM ;

Brettel, K .

NATURE, 2000, 405 (6786) :586-590

[3] Redox properties of the PutA protein from Escherichia coli and the influence of the flavin redox state on PutA-DNA interactions [J].

Becker, DF ;

Thomas, EA .

BIOCHEMISTRY, 2001, 40 (15) :4714-4721

[4] Dissociative electron transfer to and from pyrimidine cyclobutane dimers:: An electrochemical study [J].

Boussicault, F ;

Krüger, O ;

Robert, M ;

Wille, U .

ORGANIC & BIOMOLECULAR CHEMISTRY, 2004, 2 (19) :2742-2750

[5] Dissection of the triple tryptophan electron transfer chain in Escherichial coli DNA photolyase:: Trp382 is the primary donor in photoactivation [J].

Byrdin, M ;

Eker, APM ;

Vos, MH ;

Brettel, K .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (15) :8676-8681

[6]

Dutton P L, 1978, Methods Enzymol, V54, P411

[7] STUDIES OF ELECTRON-TRANSFER PROPERTIES OF SALICYLATE HYDROXYLASE FROM PSEUDOMONAS-CEPACIA AND EFFECTS OF SALICYLATE AND BENZOATE BINDING [J].

EINARSDOTTIR, GH ;

STANKOVICH, MT ;

TU, SC .

BIOCHEMISTRY, 1988, 27 (09) :3277-3285

[8] Role of critical charged residues in reduction potential modulation of ferredoxin-NADP+ reductase -: Differential stabilization of FAD redox forms [J].

Faro, M ;

Gómez-Moreno, C ;

Stankovich, M ;

Medina, M .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 2002, 269 (11) :2656-2661

[9] Potentiometric analysis of UDP-galactopyranose mutase: Stabilization of the flavosemiquinone by substrate [J].

Fullerton, SWB ;

Daff, S ;

Sanders, DAR ;

Ingledew, WJ ;

Whitfield, C ;

Chapman, SK ;

Naismith, JH .

BIOCHEMISTRY, 2003, 42 (07) :2104-2109

[10] Origin of the transient electron paramagnetic resonance signals in DNA photolyase [J].

Gindt, YM ;

Vollenbroek, E ;

Westphal, K ;

Sackett, H ;

Sancar, A ;

Babcock, GT .

BIOCHEMISTRY, 1999, 38 (13) :3857-3866

← 1 2 3 4 5 →