(Q57654204)

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Resonance Raman spectroscopic study of the neutral flavin radical complex of DNA photolyase fromEscherichia coli

article published in 2001

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Resonance Raman spectroscopic study of the neutral flavin radical complex of DNA photolyase fromEscherichia coli (English)

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Daniel H. Murgida

1

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Peter Hildebrandt

object named as

Peter Hildebrandt

series ordinal

5

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Adelbert Bacher

series ordinal

3

object named as

Adelbert Bacher

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author name string

Erik Schleicher

series ordinal

2

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Gerald Richter

series ordinal

4

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publication date

2001

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published in

Journal of Raman Spectroscopy

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volume

32

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issue

6-7

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page(s)

551-556

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cites work

Binding of Escherichia coli DNA photolyase to UV-irradiated DNA.

1 reference

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reference URL

https://api.crossref.org/works/10.1002%2FJRS.719

retrieved

21 January 2018

Effect of base, pentose, and phosphodiester backbone structures on binding and repair of pyrimidine dimers by Escherichia coli DNA photolyase

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Crossref

reference URL

https://api.crossref.org/works/10.1002%2FJRS.719

retrieved

21 January 2018

Photochemistry, photophysics, and mechanism of pyrimidine dimer repair by DNA photolyase

1 reference

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Crossref

reference URL

https://api.crossref.org/works/10.1002%2FJRS.719

retrieved

21 January 2018

The active form of Escherichia coli DNA photolyase contains a fully reduced flavin and not a flavin radical, both in vivo and in vitro.

1 reference

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Crossref

reference URL

https://api.crossref.org/works/10.1002%2FJRS.719

retrieved

21 January 2018

Crystal Structure of DNA Photolyase from Escherichia coli

1 reference

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https://api.crossref.org/works/10.1002%2FJRS.719

retrieved

21 January 2018

Crystal structure of DNA photolyase from Anacystis nidulans

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https://api.crossref.org/works/10.1002%2FJRS.719

retrieved

21 January 2018

Chromophore function and interaction in Escherichia coli DNA photolyase: reconstitution of the apoenzyme with pterin and/or flavin derivatives.

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https://api.crossref.org/works/10.1002%2FJRS.719

retrieved

21 January 2018

Time-resolved EPR studies with DNA photolyase: excited-state FADH0 abstracts an electron from Trp-306 to generate FADH-, the catalytically active form of the cofactor

1 reference

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reference URL

https://api.crossref.org/works/10.1002%2FJRS.719

retrieved

21 January 2018

Active site of DNA photolyase: tryptophan-306 is the intrinsic hydrogen atom donor essential for flavin radical photoreduction and DNA repair in vitro

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https://api.crossref.org/works/10.1002%2FJRS.719

retrieved

21 January 2018

Resonance Raman spectra of carbon-13- and nitrogen-15-labeled riboflavin bound to egg-white flavoprotein

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https://api.crossref.org/works/10.1002%2FJRS.719

retrieved

21 January 2018

Resonance Raman spectra of anionic semiquinoid form of a flavoenzyme, D-amino acid oxidase

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1002%2FJRS.719

retrieved

21 January 2018

Resonance Raman Spectroscopic Study of Phenoxyl Radical Complexes

1 reference

stated in

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reference URL

https://api.crossref.org/works/10.1002%2FJRS.719

retrieved

21 January 2018

Identifiers

DOI

10.1002/JRS.719

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(Q57654204)

Resonance Raman spectroscopic study of the neutral flavin radical complex of DNA photolyase fromEscherichia coli

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