PMID- 32615496
OWN - NLM
STAT- MEDLINE
DCOM- 20200828
LR  - 20200828
IS  - 1090-2414 (Electronic)
IS  - 0147-6513 (Linking)
VI  - 202
DP  - 2020 Oct 1
TI  - Experimental and theoretical affinity and catalysis studies between halogenated 
      phenols and peroxidases: Understanding the bioremediation potential.
PG  - 110895
LID - S0147-6513(20)30734-X [pii]
LID - 10.1016/j.ecoenv.2020.110895 [doi]
AB  - Halogenated phenols, such as 2,4-dichlorophenol (2,4-DCP) and 4-bromophenol 
      (4-BP) are pollutants generated by a various industrial sectors like chemical, 
      dye, paper bleaching, pharmaceuticals or in an agriculture as pesticides. The use 
      of Horseradish peroxidase (HRP) in the halogenated phenols treatment has already 
      been mentioned, but it is not well understood how the different phenolic 
      substrates can bind in the peroxidase active site nor how these specific 
      interactions can influence in the bioremediation potential. In this work, 
      different removal efficiencies were obtained for phenolic compounds investigated 
      using HRP as catalyst (93.87 and 59.19% to 4BP and 2,4 DCP, respectively). Thus, 
      to rationalize this result based on the interactions of phenols with active 
      center of HRP, we combine computational and experimental methodologies. The 
      theoretical approaches utilized include density functional theory (DFT) 
      calculations, docking simulation and quantum mechanics/molecular mechanics 
      (QM/MM) technique. Michaelis Menten constant (Km) obtained through experimental 
      methodologies were 2.3 and 0.95 mM to 2,4-DCP and 4-BP, respectively, while the 
      specificity constant (K(cat)/K(m)) found was 1.44 mM(-1) s(-1) and 
      0.62 mM(-1) s(-1) for 4-BP and 2,4-DCP, respectively. The experimental parameters 
      appointed to the highest affinity of HRP to 4-BP. According to the molecular 
      docking calculations, both ligands have shown stabilizing intermolecular 
      interaction energies within the HRP active site, however, the 4-BP showed more 
      stabilizing interaction energy (-53.00 kcal mol(-1)) than 2,4-dichlorophenol 
      (-49.23 kcal mol(-1)). Besides that, oxidative mechanism of 4-BP and 2,4-DCP was 
      investigated by the hybrid QM/MM approach. This study showed that the lowest 
      activation energy values for transition states investigated were obtained for 
      4-BP. Therefore, by theoretical approach, the compound 4-BP showed the more 
      stabilizing interaction and activation energy values related to the interaction 
      within the enzyme and the oxidative reaction mechanism, respectively, which 
      corroborates with experimental parameters obtained. The combination between 
      experimental and theoretical approaches was essential to understand how the 
      degradation potential of the HRP enzyme depends on the interactions between 
      substrate and the active center cavity of the enzyme.
CI  - Copyright (c) 2020 Elsevier Inc. All rights reserved.
FAU - Bretz, Raphael Resende
AU  - Bretz RR
AD  - Department of Natural Sciences (DCNAT), Federal University of Sao Joao del-Rei, 
      Sao Joao del Rei, Brazil.
FAU - de Castro, Alexandre A
AU  - de Castro AA
AD  - Department of Chemistry, Federal University of Lavras, Lavras, Brazil.
FAU - Lara Ferreira, Igor F
AU  - Lara Ferreira IF
AD  - Department of Natural Sciences (DCNAT), Federal University of Sao Joao del-Rei, 
      Sao Joao del Rei, Brazil.
FAU - Ramalho, Teodorico C
AU  - Ramalho TC
AD  - Department of Chemistry, Federal University of Lavras, Lavras, Brazil; Department 
      of Chemistry, Faculty of Science, University of Hradec Kralove, Hradec Kralove, 
      Czech Republic.
FAU - Silva, Maria Cristina
AU  - Silva MC
AD  - Department of Natural Sciences (DCNAT), Federal University of Sao Joao del-Rei, 
      Sao Joao del Rei, Brazil. Electronic address: crisiria@ufsj.edu.br.
LA  - eng
PT  - Journal Article
DEP - 20200629
PL  - Netherlands
TA  - Ecotoxicol Environ Saf
JT  - Ecotoxicology and environmental safety
JID - 7805381
RN  - 0 (Environmental Pollutants)
RN  - 0 (Phenols)
RN  - EC 1.11.1.- (Horseradish Peroxidase)
RN  - EC 1.11.1.- (Peroxidases)
RN  - LAO4J0183I (4-bromophenol)
SB  - IM
MH  - *Biodegradation, Environmental
MH  - Catalysis
MH  - Environmental Pollutants
MH  - Horseradish Peroxidase/chemistry
MH  - Kinetics
MH  - Molecular Docking Simulation
MH  - Oxidation-Reduction
MH  - Peroxidases/*metabolism
MH  - Phenols/*metabolism
OTO - NOTNLM
OT  - Experimental techniques
OT  - HRP
OT  - Halogenated phenols
OT  - Theoretical calculations
EDAT- 2020/07/03 06:00
MHDA- 2020/08/29 06:00
CRDT- 2020/07/03 06:00
PHST- 2020/02/06 00:00 [received]
PHST- 2020/06/08 00:00 [revised]
PHST- 2020/06/12 00:00 [accepted]
PHST- 2020/07/03 06:00 [pubmed]
PHST- 2020/08/29 06:00 [medline]
PHST- 2020/07/03 06:00 [entrez]
AID - S0147-6513(20)30734-X [pii]
AID - 10.1016/j.ecoenv.2020.110895 [doi]
PST - ppublish
SO  - Ecotoxicol Environ Saf. 2020 Oct 1;202:110895. doi: 10.1016/j.ecoenv.2020.110895. 
      Epub 2020 Jun 29.