Substrate electric dipole moment exerts a pH-dependent effect on electron transfer in Escherichia coli photolyase

Sofia M. Kapetanaki, Meghan Ramsey, Yvonne Gindt, Johannes Schelvis

Research output: Contribution to journalArticleResearchpeer-review

20 Citations (Scopus)

Abstract

Transient absorption spectroscopy is used to demonstrate that the electric dipole moment of the substrate cyclobutane thymine dimer affects the charge recombination reaction between fully reduced flavin adenine dinucleotide (FADH-) and the neutral radical tryptophan 306 (Trp306•) in Escherichia coli DNA photolyase. At pH 7.4, the charge recombination is slowed by a factor of 1.75 in the presence of substrate, but not at pH 5.4. Photolyase does bind substrate at pH 5.4, and it seems that this pH effect originates from the conversion of FADH- to FADH2 at lower pH. The free-energy changes calculated from the electric field parameters and from the change in electron transfer rate are in good agreement and support the idea that the substrate electric dipole is responsible for the observed change in electron transfer rate. It is expected that the substrate electric field will also modify the physiologically important from excited 1FADH- to the substrate in the DNA repair reaction.

Original languageEnglish
Pages (from-to)6214-6215
Number of pages2
JournalJournal of the American Chemical Society
Volume126
Issue number20
DOIs
StatePublished - 26 May 2004

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Deoxyribodipyrimidine Photo-Lyase
Electric dipole moments
Escherichia coli
Electrons
Substrates
Electric fields
pH effects
Pyrimidine Dimers
Flavin-Adenine Dinucleotide
Absorption spectroscopy
Tryptophan
Free energy
Repair
DNA

Cite this

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title = "Substrate electric dipole moment exerts a pH-dependent effect on electron transfer in Escherichia coli photolyase",
abstract = "Transient absorption spectroscopy is used to demonstrate that the electric dipole moment of the substrate cyclobutane thymine dimer affects the charge recombination reaction between fully reduced flavin adenine dinucleotide (FADH-) and the neutral radical tryptophan 306 (Trp306•) in Escherichia coli DNA photolyase. At pH 7.4, the charge recombination is slowed by a factor of 1.75 in the presence of substrate, but not at pH 5.4. Photolyase does bind substrate at pH 5.4, and it seems that this pH effect originates from the conversion of FADH- to FADH2 at lower pH. The free-energy changes calculated from the electric field parameters and from the change in electron transfer rate are in good agreement and support the idea that the substrate electric dipole is responsible for the observed change in electron transfer rate. It is expected that the substrate electric field will also modify the physiologically important from excited 1FADH- to the substrate in the DNA repair reaction.",
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Substrate electric dipole moment exerts a pH-dependent effect on electron transfer in Escherichia coli photolyase. / Kapetanaki, Sofia M.; Ramsey, Meghan; Gindt, Yvonne; Schelvis, Johannes.

In: Journal of the American Chemical Society, Vol. 126, No. 20, 26.05.2004, p. 6214-6215.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Substrate electric dipole moment exerts a pH-dependent effect on electron transfer in Escherichia coli photolyase

AU - Kapetanaki, Sofia M.

AU - Ramsey, Meghan

AU - Gindt, Yvonne

AU - Schelvis, Johannes

PY - 2004/5/26

Y1 - 2004/5/26

N2 - Transient absorption spectroscopy is used to demonstrate that the electric dipole moment of the substrate cyclobutane thymine dimer affects the charge recombination reaction between fully reduced flavin adenine dinucleotide (FADH-) and the neutral radical tryptophan 306 (Trp306•) in Escherichia coli DNA photolyase. At pH 7.4, the charge recombination is slowed by a factor of 1.75 in the presence of substrate, but not at pH 5.4. Photolyase does bind substrate at pH 5.4, and it seems that this pH effect originates from the conversion of FADH- to FADH2 at lower pH. The free-energy changes calculated from the electric field parameters and from the change in electron transfer rate are in good agreement and support the idea that the substrate electric dipole is responsible for the observed change in electron transfer rate. It is expected that the substrate electric field will also modify the physiologically important from excited 1FADH- to the substrate in the DNA repair reaction.

AB - Transient absorption spectroscopy is used to demonstrate that the electric dipole moment of the substrate cyclobutane thymine dimer affects the charge recombination reaction between fully reduced flavin adenine dinucleotide (FADH-) and the neutral radical tryptophan 306 (Trp306•) in Escherichia coli DNA photolyase. At pH 7.4, the charge recombination is slowed by a factor of 1.75 in the presence of substrate, but not at pH 5.4. Photolyase does bind substrate at pH 5.4, and it seems that this pH effect originates from the conversion of FADH- to FADH2 at lower pH. The free-energy changes calculated from the electric field parameters and from the change in electron transfer rate are in good agreement and support the idea that the substrate electric dipole is responsible for the observed change in electron transfer rate. It is expected that the substrate electric field will also modify the physiologically important from excited 1FADH- to the substrate in the DNA repair reaction.

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