English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Neutral histidine and photoinduced electron transfer in DNA photolyases

Domratcheva, T. (2011). Neutral histidine and photoinduced electron transfer in DNA photolyases. Journal of the American Chemical Society, 133(45), 18172-18182. doi:10.1021/ja203964d.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-11B3-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-11B4-3
Genre: Journal Article
Alternative Title : Neutral histidine and photoinduced electron transfer in DNA photolyases

Files

show Files
hide Files
:
JACS_133_ 2011_18172.pdf (Any fulltext), 2MB
 
File Permalink:
-
Name:
JACS_133_ 2011_18172.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-
Locator:
http://dx.doi.org/10.1021/ja203964d (Any fulltext)
Description:
-

Creators

show
hide
 Creators:
Domratcheva, Tatiana1, Author              
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

Content

show
hide
Free keywords: -
 Abstract: The two major UV−induced DNA lesions, the cyclobutane pyrimidine dimers (CPD) and (6−4) pyrimidine−pyrimidone photoproducts, can be repaired by the light−activated enzymes CPD and (6−4) photolyases, respectively. It is a long−standing question how the two classes of photolyases with alike molecular structure are capable of reversing the two chemically different DNA photoproducts. In both photolyases the repair reaction is initiated by photoinduced electron transfer from the hydroquinone−anion part of the flavin adenine dinucleotide (FADH−) cofactor to the photoproduct. Here, the state−of−the−art XMCQDPT2−CASSCF approach was employed to compute the excitation spectra of the respective active site models. It is found that protonation of His365 in the presence of the hydroquinone−anion electron donor causes spontaneous, as opposed to photoinduced, coupled proton and electron transfer to the (6−4) photoproduct. The resulting neutralized biradical, containing the neutral semiquinone and the N3'−protonated (6−4) photoproduct neutral radical, corresponds to the lowest energy electronic ground−state minimum. The high electron affinity of the N3'−protonated (6−4) photoproduct underlines this finding. Thus, it is anticipated that the (6−4) photoproduct repair is assisted by His365 in its neutral form, which is in contrast to the repair mechanisms proposed in the literature. The repair via hydroxyl group transfer assisted by neutral His365 is considered. The repair involves the 5'base radical anion of the (6−4) photoproduct which in terms of electronic structure is similar to the CPD radical anion. A unified model of the CPD and (6−4) photoproduct repair is proposed

Details

show
hide
Language(s): eng - English
 Dates: 2011-04-292011-10-032011-10-032011-11-16
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: eDoc: 664448
DOI: 10.1021/ja203964d
Other: 7730
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of the American Chemical Society
  Other : J. Am. Chem. Soc.
  Abbreviation : JACS
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: American Chemical Society
Pages: - Volume / Issue: 133 (45) Sequence Number: - Start / End Page: 18172 - 18182 Identifier: ISSN: 0002-7863
CoNE: https://pure.mpg.de/cone/journals/resource/954925376870