Crossref journal-article
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences (341)
Abstract

Photolyases repair pyrimidine dimers in DNA by converting the light energy of 300- to 500-nm photons into chemical energy. Enzymes from various organisms contain two chromophore cofactors (FADH2 and either methenyltetrahydrofolate or 8-hydroxy-5-deazaflavin) that absorb the low-energy photons and initiate splitting of the cyclobutane ring by a radical mechanism. Here, we show that, in addition to these two chromophores, in the far UV range, direct excitation of one specific tryptophan residue (out of 15 total) in the polypeptide chain of Escherichia coli photolyase leads to splitting of the cyclobutane ring with high quantum yield (phi = 0.56), independent of the other chromophores. The specific tryptophan residue responsible for photosensitized repair was identified as Trp-277 by site-specific mutagenesis.

Authors 3
  1. S T Kim (first)
  2. Y F Li (additional)
  3. A Sancar (additional)
References 0 Referenced 50

None

Dates
Type When
Created 19 years, 3 months ago (May 31, 2006, 8:15 a.m.)
Deposited 3 years, 4 months ago (April 13, 2022, 1:34 p.m.)
Indexed 1 year, 2 months ago (June 12, 2024, 9:17 a.m.)
Issued 33 years, 7 months ago (Feb. 1, 1992)
Published 33 years, 7 months ago (Feb. 1, 1992)
Published Online 33 years, 7 months ago (Feb. 1, 1992)
Published Print 33 years, 7 months ago (Feb. 1, 1992)
Funders 0

None

@article{Kim_1992, title={The third chromophore of DNA photolyase: Trp-277 of Escherichia coli DNA photolyase repairs thymine dimers by direct electron transfer.}, volume={89}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.89.3.900}, DOI={10.1073/pnas.89.3.900}, number={3}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Kim, S T and Li, Y F and Sancar, A}, year={1992}, month=feb, pages={900–904} }