Interactions of carbon nanotubes and/or graphene with manganese peroxidase during biodegradation of endocrine disruptors and triclosan

Chemosphere

Volumn 184, Issue , 2017, Pages 127-136

  Chen, Ming ^a   Zeng, Guangming ^a   Lai, Cui ^a   Zhang, Chang ^a   Xu, Piao ^a   Yan, Min ^a   Xiong, Weiping ^a  

^a HUNAN UNIVERSITY   (China)

Author keywords

Biodegradation; Carbon nanotube; Endocrine disruptors; Graphene; Personal care products

Indexed keywords

BINDING ENERGY; BIODEGRADATION; CARBON NANOTUBES; GRAPHENE; MANGANESE; MOLECULES; NANOTUBES; PHENOLS; RISK ASSESSMENT; SINGLE-WALLED CARBON NANOTUBES (SWCN); WATER POLLUTION;

BIODEGRADATION PROCESS; DIFFERENT EFFECTS; ENDOCRINE DISRUPTOR; MANGANESE PEROXIDASE; OVERALL STABILITIES; PERSONAL CARE PRODUCTS; SENSITIVE REGIONS; SINGLEWALLED CARBON NANOTUBE (SWCNT);

MANGANESE COMPOUNDS;

4,4' ISOPROPYLIDENEDIPHENOL; CARBON NANOTUBE; ENDOCRINE DISRUPTOR; GRAPHENE; MANGANESE PEROXIDASE; NONYLPHENOL; SINGLE WALLED NANOTUBE; TRICLOSAN; WATER; BENZHYDRYL DERIVATIVE; GRAPHITE; PEROXIDASE; PHENOL DERIVATIVE;

ANTIMICROBIAL ACTIVITY; BIODEGRADATION; CARBON; CARBON NANOTUBE; ENDOCRINE DISRUPTOR; ENZYME ACTIVITY; MOLECULAR ANALYSIS; PPCP;

ARTICLE; BIODEGRADATION; HYDROGEN BOND; NONHUMAN; BIOREMEDIATION; CHEMICAL MODEL; CHEMISTRY; METABOLISM;

BENZHYDRYL COMPOUNDS; BIODEGRADATION, ENVIRONMENTAL; ENDOCRINE DISRUPTORS; GRAPHITE; MODELS, CHEMICAL; NANOTUBES, CARBON; PEROXIDASES; PHENOLS; TRICLOSAN;

EID: 85019997688     PISSN: 00456535     EISSN: 18791298     Source Type: Journal    
DOI: 10.1016/j.chemosphere.2017.05.162     Document Type: Article

References (63)

1. Akhavan, O., Ghaderi, E., Toxicity of graphene and graphene oxide nanowalls against bacteria. Acs Nano 4 (2010), 5731–5736.
2. Anwar, M.A., Panneerselvam, S., Shah, M., Choi, S., Insights into the species-specific TLR4 signaling mechanism in response to Rhodobacter sphaeroides lipid A detection. Sci. Rep. Uk, 5, 2015, 7657.
3. Awasthi, M., Jaiswal, N., Singh, S., Pandey, V.P., Dwivedi, U.N., Molecular docking and dynamics simulation analyses unraveling the differential enzymatic catalysis by plant and fungal laccases with respect to lignin biosynthesis and degradation. J. Biomol. Struct. Dyn. 33 (2015), 1835–1849.
4. Bhattacherjee, A., Mandal, R.S., Das, S., Kundu, S., Sequence and 3D structure based analysis of TNT degrading proteins in Arabidopsis thaliana. J. Mol. Model, 20, 2014, 2174.
5. Cabana, H., Jiwan, J.-L.H., Rozenberg, R., Elisashvili, V., Penninckx, M., Agathos, S.N., Jones, J.P., Elimination of endocrine disrupting chemicals nonylphenol and bisphenol A and personal care product ingredient triclosan using enzyme preparation from the white rot fungus Coriolopsis polyzona. Chemosphere 67 (2007), 770–778.
6. Cabana, H., Jones, J., Agathos, S.N., Elimination of endocrine disrupting chemicals using white rot fungi and their lignin modifying enzymes: a review. Eng. Life Sci. 7 (2007), 429–456.
7. Cajthaml, T., Biodegradation of endocrine-disrupting compounds by ligninolytic fungi: mechanisms involved in the degradation. Environ. Microbiol. 17 (2015), 4822–4834.
8. Calvaresi, M., Hoefinger, S., Zerbetto, F., Probing the structure of lysozyme-carbon-nanotube hybrids with molecular dynamics. Chem. Eur. J. 18 (2012), 4308–4313.
9. Cappel, D., Wahlstro¨m, R., Brenk, R., Sotriffer, C.A., Probing the dynamic nature of water molecules and their influences on ligand binding in a model binding site. J. Chem. Inf. Model 51 (2011), 2581–2594.
10. Chen, M., Qin, X., Li, J., Zeng, G., Probing molecular basis of single-walled carbon nanotube degradation and nondegradation by enzymes based on manganese peroxidase and lignin peroxidase. RSC Adv. 6 (2016), 3592–3599.
11. Chen, M., Qin, X., Zeng, G., Single-walled carbon nanotube release affects the microbial enzyme-catalyzed oxidation processes of organic pollutants and lignin model compounds in nature. Chemosphere 163 (2016), 217–226.
12. Chen, M., Qin, X., Zeng, G., Biodegradation of carbon nanotubes, graphene, and their derivatives. Trends Biotechnol., 2017, 10.1016/j.tibtech.2016.1012.1001.
13. Chen, M., Xu, P., Zeng, G., Yang, C., Huang, D., Zhang, J., Bioremediation of soils contaminated with polycyclic aromatic hydrocarbons, petroleum, pesticides, chlorophenols and heavy metals by composting: applications, microbes and future research needs. Biotechnol. Adv. 33 (2015), 745–755.
14. Chen, M., Zeng, G., Tan, Z., Jiang, M., Li, H., Liu, L., Zhu, Y., Yu, Z., Wei, Z., Liu, Y., Xie, G., Understanding lignin-degrading reactions of ligninolytic enzymes: binding affinity and interactional profile. Plos One, 6, 2011, e25647.
15. Chen, M., Zeng, G., Xu, P., Zhang, Y., Jiang, D., Zhou, S., Understanding enzymatic degradation of single-walled carbon nanotubes triggered by functionalization using molecular dynamics simulation. Environ. Sci. Nano 4 (2017), 720–727.
16. Chen, M., Zeng, G.M., Lai, C., Li, J., Xu, P., Wu, H.P., Molecular basis of laccase bound to lignin: insight from comparative studies on the interaction of Trametes versicolor laccase with various lignin model compounds. Rsc Adv. 5 (2015), 52307–52313.
17. Fürhacker, M., Scharf, S., Weber, H., Bisphenol A: emissions from point sources. Chemosphere 41 (2000), 751–756.
18. Feng, Y., Gong, J.-L., Zeng, G.-M., Niu, Q.-Y., Zhang, H.-Y., Niu, C.-G., Deng, J.-H., Yan, M., Adsorption of Cd (II) and Zn (II) from aqueous solutions using magnetic hydroxyapatite nanoparticles as adsorbents. Chem. Eng. J. 162 (2010), 487–494.
19. Gong, J.-L., Wang, B., Zeng, G.-M., Yang, C.-P., Niu, C.-G., Niu, Q.-Y., Zhou, W.-J., Liang, Y., Removal of cationic dyes from aqueous solution using magnetic multi-wall carbon nanotube nanocomposite as adsorbent. J. Hazard Mater. 164 (2009), 1517–1522.
20. Haque, N., Prabhu, N., Insights into protein–TNS (2-p-toluidinylnaphthalene-6-sulfonate) interaction using molecular dynamics simulation. J. Mol. Struct. 1068 (2014), 261–269.
21. Hermanová, S., Zarevúcká, M., Bouša, D., Pumera, M., Sofer, Z., Graphene oxide immobilized enzymes show high thermal and solvent stability. Nanoscale 7 (2015), 5852–5858.
22. Hess, B., Kutzner, C., van der Spoel, D., Lindahl, E., Gromacs 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 4 (2008), 435–447.
23. Hirano, T., Honda, Y., Watanabe, T., Kuwahara, M., Degradation of bisphenol A by the lignin-degrading enzyme, manganese peroxidase, produced by the white-rot basidiomycete, Pleurotus ostreatus. Biosci. Biotechnol. Biochem. 64 (2000), 1958–1962.
24. Huang, D.L., Zeng, G., Feng, C.L., Hu, S., Jiang, X.Y., Tang, L., Su, F.F., Zhang, Y., Zeng, W., Liu, H.L., Degradation of lead-contaminated lignocellulosic waste by Phanerochaete chrysosporium and the reduction of lead toxicity. Environ. Sci. Technol. 42 (2008), 4946–4951.
25. Humphrey, W., Dalke, A., Schulten, K., VMD: visual molecular dynamics. J. Mol. Graph 14 (1996), 33–38.
26. Hundt, K., Martin, D., Hammer, E., Jonas, U., Kindermann, M.K., Schauer, F., Transformation of triclosan by Trametes versicolor and Pycnoporus cinnabarinus. Appl. Environ. Microb. 66 (2000), 4157–4160.
27. Inoue, Y., Hata, T., Kawai, S., Okamura, H., Nishida, T., Elimination and detoxification of triclosan by manganese peroxidase from white rot fungus. J. Hazard Mater. 180 (2010), 764–767.
28. Kaminski, G.A., Friesner, R.A., Tirado-Rives, J., Jorgensen, W.L., Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides. J. Phys. Chem. B 105 (2001), 6474–6487.
29. Kandt, C., Schlitter, J., Gerwert, K., Dynamics of water molecules in the bacteriorhodopsin trimer in explicit lipid/water environment. Biophys. J. 86 (2004), 705–717.
30. Kang, J.-H., Katayama, Y., Kondo, F., Biodegradation or metabolism of bisphenol A: from microorganisms to mammals. Toxicology 217 (2006), 81–90.
31. Kasprzyk-Hordern, B., Dinsdale, R.M., Guwy, A.J., The removal of pharmaceuticals, personal care products, endocrine disruptors and illicit drugs during wastewater treatment and its impact on the quality of receiving waters. Water Res. 43 (2009), 363–380.
32. Kim, S., Thiessen, P.A., Bolton, E.E., Chen, J., Fu, G., Gindulyte, A., Han, L., He, J., He, S., Shoemaker, B.A., Wang, J., Yu, B., Zhang, J., Bryant, S.H., PubChem Substance and Compound databases. Nucleic Acids Res. 44 (2016), D1202–D1213.
33. Kim, Y.-J., Nicell, J.A., Impact of reaction conditions on the laccase-catalyzed conversion of bisphenol A. Bioresour. Technol. 97 (2006), 1431–1442.
34. Kim, Y., Yeo, S., Song, H.-G., Choi, H.T., Enhanced expression of laccase during the degradation of endocrine disrupting chemicals in Trametes versicolor. J. Microbiol. 46 (2008), 402–407.
35. Korsman, J.C., Schipper, A.M., de Vos, M.G., van den Heuvel-Greve, M.J., Vethaak, A.D., de Voogt, P., Hendriks, A.J., Modeling bioaccumulation and biomagnification of nonylphenol and its ethoxylates in estuarine–marine food chains. Chemosphere 138 (2015), 33–39.
36. Kotchey, G.P., Gaugler, J.A., Kapralov, A.A., Kagan, V.E., Star, A., Effect of antioxidants on enzyme-catalysed biodegradation of carbon nanotubes. J. Mater. Chem. B 1 (2013), 302–309.
37. Kumar, K.M., Anbarasu, A., Ramaiah, S., Molecular docking and molecular dynamics studies on beta-lactamases and penicillin binding proteins. Mol. Biosyst. 10 (2014), 891–900.
38. Kumari, R., Kumar, R., Lynn, A., Consort, O.S.D.D., g_mmpbsa-A GROMACS tool for high-throughput MM-PBSA calculations. J. Chem. Inf. Model 54 (2014), 1951–1962.
39. Li, Z., Lazaridis, T., Water at biomolecular binding interfaces. Phys. Chem. Chem. Phys. 9 (2007), 573–581.
40. Mashiach, E., Schneidman-Duhovny, D., Andrusier, N., Nussinov, R., Wolfson, H.J., FireDock: a web server for fast interaction refinement in molecular docking. Nucleic Acids Res. 36 (2008), W229–W232.
41. Mubarak, N., Wong, J., Tan, K., Sahu, J., Abdullah, E., Jayakumar, N., Ganesan, P., Immobilization of cellulase enzyme on functionalized multiwall carbon nanotubes. J. Mol. Catal. B Enzym 107 (2014), 124–131.
42. Omotuyi, I.O., Ebola virus envelope glycoprotein derived peptide in human Furin-bound state: computational studies. J. Biomol. Struct. Dyn. 33 (2015), 461–470.
43. Pence, H.E., Williams, A., ChemSpider: an online chemical information resource. J. Chem. Educ. 87 (2010), 1123–1124.
44. Pronk, S., Páll, S., Schulz, R., Larsson, P., Bjelkmar, P., Apostolov, R., Shirts, M.R., Smith, J.C., Kasson, P.M., van der Spoel, D., GROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit. Bioinformatics 29 (2013), 845–854.
45. Rajesh, C., Majumder, C., Mizuseki, H., Kawazoe, Y., A theoretical study on the interaction of aromatic amino acids with graphene and single walled carbon nanotube. J. Chem. Phys., 130, 2009, 124911.
46. Rodrigues, D.F., Jaisi, D.P., Elimelech, M., Toxicity of functionalized single-walled carbon nanotubes on soil microbial communities: implications for nutrient cycling in soil. Environ. Sci. Technol. 47 (2013), 625–633.
47. Rose, P.W., Bi, C., Bluhm, W.F., Christie, C.H., Dimitropoulos, D., Dutta, S., Green, R.K., Goodsell, D.S., Prlić, A., Quesada, M., The RCSB Protein Data Bank: new resources for research and education. Nucleic Acids Res. 41 (2013), D475–D482.
48. Schneidman-Duhovny, D., Inbar, Y., Nussinov, R., Wolfson, H.J., PatchDock and SymmDock: servers for rigid and symmetric docking. Nucleic Acids Res. 33 (2005), W363–W367.
49. Sundaramoorthy, M., Gold, M.H., Poulos, T.L., Ultrahigh (0.93 angstrom) resolution structure of manganese peroxidase from Phanerochaete chrysosporium: implications for the catalytic mechanism. J. Inorg. Biochem. 104 (2010), 683–690.
50. Sundaramoorthy, M., Youngs, H.L., Gold, M.H., Poulos, T.L., High-resolution crystal structure of manganese peroxidase: substrate and inhibitor complexes. Biochem. Us 44 (2005), 6463–6470.
51. Takamiya, M., Magan, N., Warner, P.J., Impact assessment of bisphenol A on lignin-modifying enzymes by basidiomycete Trametes versicolor. J. Hazard Mater. 154 (2008), 33–37.
52. Thomsen, R., Christensen, M.H., MolDock: a new technique for high-accuracy molecular docking. J. Med. Chem. 49 (2006), 3315–3321.
53. Tsutsumi, Y., Haneda, T., Nishida, T., Removal of estrogenic activities of bisphenol A and nonylphenol by oxidative enzymes from lignin-degrading basidiomycetes. Chemosphere 42 (2001), 271–276.
54. Uguz, C., Iscan, M., Ergüven, A., Isgor, B., Togan, I., The bioaccumulation of nonyphenol and its adverse effect on the liver of rainbow trout (Onchorynchus mykiss). Environ. Res. 92 (2003), 262–270.
55. Vazquez-Duhalt, R., Marquez-Rocha, F., Ponce, E., Licea, A., Viana, M., Nonylphenol, an integrated vision of a pollutant. Appl. Ecol. Env. Res. 4 (2005), 1–25.
56. Vidal-Liñán, L., Bellas, J., Salgueiro-González, N., Muniategui, S., Beiras, R., Bioaccumulation of 4-nonylphenol and effects on biomarkers, acetylcholinesterase, glutathione-S-transferase and glutathione peroxidase, in Mytilus galloprovincialis mussel gilla. Environ. Pollut. 200 (2015), 133–139.
57. Xie, J., Ming, Z., Li, H., Yang, H., Yu, B., Wu, R., Liu, X., Bai, Y., Yang, S.-T., Toxicity of graphene oxide to white rot fungus Phanerochaete chrysosporium. Chemosphere 151 (2016), 324–331.
58. Xu, P., Zeng, G.M., Huang, D.L., Feng, C.L., Hu, S., Zhao, M.H., Lai, C., Wei, Z., Huang, C., Xie, G.X., Use of iron oxide nanomaterials in wastewater treatment: a review. Sci. Total Environ. 424 (2012), 1–10.
59. Zhang, Y., Ali, S.F., Dervishi, E., Xu, Y., Li, Z., Casciano, D., Biris, A.S., Cytotoxicity effects of graphene and single-wall carbon nanotubes in neural phaeochromocytoma-derived PC12 cells. Acs Nano 4 (2010), 3181–3186.
60. Zhang, Y., Zeng, G.-M., Tang, L., Huang, D.-L., Jiang, X.-Y., Chen, Y.-N., A hydroquinone biosensor using modified core–shell magnetic nanoparticles supported on carbon paste electrode. Biosens. Bioelectron. 22 (2007), 2121–2126.
61. Zhao, J., Wang, Z., White, J.C., Xing, B., Graphene in the aquatic environment: adsorption, dispersion, toxicity and transformation. Environ. Sci. Technol. 48 (2014), 9995–10009.
62. Zhao, M., Zhang, C., Zeng, G., Huang, D., Xu, P., Cheng, M., Growth, metabolism of Phanerochaete chrysosporium and route of lignin degradation in response to cadmium stress in solid-state fermentation. Chemosphere 138 (2015), 560–567.
63. Zoete, V., Meuwly, M., Karplus, M., Study of the insulin dimerization: binding free energy calculations and per-residue free energy decomposition. Proteins 61 (2005), 79–93.