Substrate binding modulates the reduction potential of DNA photolyase

Yvonne M. Gindt; Johannes P.M. Schelvis; Katie L. Thoren; Tina H. Huang

doi:10.1021/ja051441r

Substrate binding modulates the reduction potential of DNA photolyase

Yvonne M. Gindt, Johannes P.M. Schelvis, Katie L. Thoren, Tina H. Huang

Chemistry and Biochemistry

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

39 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	10472-10473
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	127
Issue number	30
DOIs	https://doi.org/10.1021/ja051441r
State	Published - 3 Aug 2005

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title = "Substrate binding modulates the reduction potential of DNA photolyase",

abstract = "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.",

author = "Gindt, {Yvonne M.} and Schelvis, {Johannes P.M.} and Thoren, {Katie L.} and Huang, {Tina H.}",

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T1 - Substrate binding modulates the reduction potential of DNA photolyase

AU - Gindt, Yvonne M.

AU - Schelvis, Johannes P.M.

AU - Thoren, Katie L.

AU - Huang, Tina H.

PY - 2005/8/3

Y1 - 2005/8/3

N2 - 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.

AB - 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.

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M3 - Article

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VL - 127

SP - 10472

EP - 10473

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 30

ER -

Substrate binding modulates the reduction potential of DNA photolyase

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