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Denumirea produsului Etanol 96% EMPROVE® EXPERT Ph Eur,BP The life science business of Merck
operates as MilliporeSigma in the US and Canada Pagina 22 aparţinând 34 ERC2 Formularea de
preparate ERC4 Utilizarea industrială a aditivilor de prelucrare în procese şi produse, fără a deveni parte
din articole ERC6a Utilizare industrială care duce la fabricarea altei substanţe (utilizarea intermediarilor)
2. Scenariu contributiv: conditii de utilizare şi masuri de managementul ri scului. 2.1 Scenariu
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
condiţii de operare indicate ce ar afecta expunerea mediului înconjurător Numărul de zile de emisie pe
an 350 Factor de emisie sau eliberare: aer 70 % Factor de emisie sau eliberare: apă 87 % Condiţii şi
măsuri referitoare la staţiile de tratare a apelor uzate municipale Tipul staţiei de epurare a apelor uzate
Staţie de tratare/epurare a apelor uzate municipală Eficienţa (pentru o măsurătoare) 90 % 2.2 Scenariu
contribuind la controlul expunerii mediului la:: ERC2 Cantitatea folosită Cantitatea anuală per sit 75000 t
Factorii de mediu ce nu sunt influenţaţi de gestiunea riscurilor
PMID: 28802828
PMCID: PMC5650541
DOI: 10.1016/j.abb.2017.08.007
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.