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din articole ERC6a Utilizare industrială care duce la fabricarea altei substanţe (utilizarea intermediarilor)
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contribuind la controlul expunerii mediului la:: ERC1, ERC4, ERC6a Cantitatea folosită Cantitatea anuală
per sit 400000 t Factorii de mediu ce nu sunt influenţaţi de gestiunea riscurilor Debit 18.000 m3/d Alte
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Factorii de mediu ce nu sunt influenţaţi de gestiunea riscurilor

Photolyase: Dynamics and Electron-


Transfer Mechanisms of DNA Repair
Meng Zhang 1, Lijuan Wang 1, Dongping Zhong 2
Affiliations expand

 PMID: 28802828

 PMCID: PMC5650541

 DOI: 10.1016/j.abb.2017.08.007

Free PMC article

Abstract
Photolyase, a flavoenzyme containing flavin adenine dinucleotide (FAD) molecule as a
catalytic cofactor, repairs UV-induced DNA damage of cyclobutane pyrimidine dimer
(CPD) and pyrimidine-pyrimidone (6-4) photoproduct using blue light. The FAD cofactor,
conserved in the whole protein superfamily of photolyase/cryptochromes, adopts a
unique folded configuration at the active site that plays a critical functional role in DNA
repair. Here, we review our comprehensive characterization of the dynamics of flavin
cofactor and its repair photocycles by different classes of photolyases on the most
fundamental level. Using femtosecond spectroscopy and molecular biology, significant
advances have recently been made to map out the entire dynamical evolution and
determine actual timescales of all the catalytic processes in photolyases. The repair of
CPD reveals seven electron-transfer (ET) reactions among ten elementary steps by a
cyclic ET radical mechanism through bifurcating ET pathways, a direct tunneling route
mediated by the intervening adenine and a two-step hopping path bridged by the
intermediate adenine from the cofactor to damaged DNA, through the conserved
folded flavin at the active site. The unified, bifurcated ET mechanism elucidates the
molecular origin of various repair quantum yields of different photolyases from three life
kingdoms. For 6-4 photoproduct repair, a similar cyclic ET mechanism operates and a
new cyclic proton transfer with a conserved histidine residue at the active site of (6-4)
photolyases is revealed.

Keywords: DNA repair; Electron hopping; Electron tunneling; Flavoprotein photolyase;


Intraprotein electron transfer; Photocycle; Ultrafast enzyme dynamics.

Copyright © 2017 Elsevier Inc. All rights reserved.

The primary structure of DNA is constantly subjected to alteration by cellular


metabolites and exogenous DNA-damaging agents. These alterations may cause
simple base changes or they may cause more complex changes including
deletions, fusions, translocations, or aneuploidy. Such alterations may ultimately
lead to cellular death of unicellular organisms or degenerative changes and aging
of multicellular organisms.
DNA damages can perturb the cellular steady-state quasi-equilibrium and
activate or amplify certain biochemical pathways that regulate cell growth and
division and pathways that help to coordinate DNA replication with damage
removal. The four types of pathways elicited by DNA damage known, or
presumed, to ameliorate harmful damage effects are DNA repair, DNA damage
checkpoints, transcriptional response, and apoptosis (1) (Figure 1). Defects in
any of these pathways may cause genomic instability (2). This review focuses
upon the mechanisms of DNA repair and the DNA damage checkpoints.