Haloalkane dehalogenases: Biotechnological applications

Biotechnology Journal

Volumn 8, Issue 1, 2013, Pages 32-45

  Koudelakova, Tana ^a   Bidmanova, Sarka ^a   Dvorak, Pavel ^a   Pavelka, Antonin ^a   Chaloupkova, Radka ^a   Prokop, Zbynek ^a,b   Damborsky, Jiri ^a,b  

^a MASARYK UNIVERSITY   (Czech Republic)

^b Enantis Ltd   (Czech Republic)

Author keywords

Biocatalysis; Biodegradation; Biosensors; Cell imaging; Protein analysis

Indexed keywords

BIOCATALYSIS; BIOCATALYTIC PREPARATION; BIOCHEMICAL PROPERTIES; BIOSENSING; BIOTECHNOLOGICAL APPLICATIONS; BUILDING BLOCKES; CARBON-HALOGEN BOND; CATALYTIC EFFICIENCIES; CATALYTIC MECHANISMS; CELL IMAGING; CHEMICAL PROCESS; COSOLVENTS; ENVIRONMENTAL POLLUTANTS; HIGH ROBUSTNESS; ORGANIC SYNTHESIS; PRODUCT INHIBITION; PROTEIN ANALYSIS; PROTEIN ENGINEERING; PROTEIN TAGGING; SUBSTRATE SPECIFICITY; WARFARE AGENTS;

BIODEGRADATION; BIOREMEDIATION; BIOSENSORS; BIOSYNTHESIS; GENETIC ENGINEERING; MICROBIOLOGY; POLLUTION; SUBSTRATES;

ENZYME INHIBITION;

HALOALKANE DEHALOGENASE; HYDROLASE; UNCLASSIFIED DRUG;

BINDING AFFINITY; BIOCATALYSIS; BIOREMEDIATION; BIOTECHNOLOGY; BRADYRHIZOBIUM; BRADYRHIZOBIUM JAPONICUM; CANDIDA ANTARCTICA; ENANTIOSELECTIVITY; ENZYME ISOLATION; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; GENETIC PROCEDURES; MYCOBACTERIUM BOVIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ENGINEERING; PROTEIN EXPRESSION; PSYCHROBACTER; RECYCLING; REVIEW; RHIZOBIUM RADIOBACTER; RHODOCOCCUS; RHODOPIRELLULA; XANTHOBACTER;

ANIMALS; BIOTECHNOLOGY; HUMANS; HYDROLASES;

EID: 84871749232     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201100486     Document Type: Review

References (125)

1. Damborsky, J., Rorije, E., Jesenska, A., Nagata, Y. et al., Structure-specificity relationships for haloalkane dehalogenases. Environ. Toxicol. Chem. 2001, 20, 2681-2689.
2. Verschueren, K. H., Seljée, F., Rozeboom, H. J., Kalk, K. H., Dijkstra, B. W., Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase. Nature 1993, 363, 693-698.
3. Damborsky, J., Koca, J., Analysis of the reaction mechanism and substrate specificity of haloalkane dehalogenases by sequential and structural comparisons. Protein Eng. 1999, 12, 989-998.
4. Hardman, D. J., Biotransformation of halogenated compounds. Crit. Rev. Biotechnol. 1991, 11, 1-40.
5. Leisinger, T., Bader, R., Microbial dehalogenation of synthetic organohalogen compounds - hydrolytic dehalogenases. Chimia 1993, 47, 116-121.
6. Pries, F., Van Der Ploeg, J., Dolfing, J., Janssen, D., Degradation of halogenated aliphatic-compounds - the role of adaptation. FEMS Microbiol. Rev. 1994, 15, 279-295.
7. Fetzner, S., Lingens, F., Bacterial dehalogenases - biochemistry, genetics, and biotechnological applications. Microbiol. Rev. 1994, 58, 641-685.
8. Janssen, D. B., Pries, F., Van Der Ploeg, J. R., Genetics and biochemistry of dehalogenating enzymes. Annu. Rev. Microbiol. 1994, 48, 163-191.
9. Slater, J., Bull, A., Hardman, D., Microbial dehalogenation. Biodegradation 1995, 6, 181-189.
10. Leisinger, T., Biodegradation of chlorinated aliphatic compounds. Curr. Opin. Biotechnol. 1996, 7, 295-300.
11. Slater, J., Bull, A., Hardman, D., Microbial dehalogenation of halogenated alkanoic acids, alcohols and alkanes. Adv. Microb. Physiol. 1997, 38, 133-176.
12. Copley, S. D., Microbial dehalogenases: enzymes recruited to convert xenobiotic substrates. Curr. Opin. Chem. Biol. 1998, 2, 613-617.
13. Fetzner, S., Bacterial dehalogenation. Appl. Microbiol. Biotechnol. 1998, 50, 633-657.
14. Swanson, P., Dehalogenases applied to industrial-scale biocatalysis. Curr. Opin. Biotech. 1999, 10, 365-369.
15. Janssen, D., Oppentocht, J., Poelarends, G., Microbial dehalogenation. Curr. Opin. Biotechnol. 2001, 12, 254-258.
16. Janssen, D. B., Evolving haloalkane dehalogenases. Curr. Opin. Chem. Biol. 2004, 8, 150-159.
17. Janssen, D. B., Dinkla, I. J. T., Poelarends, G. J., Terpstra, P., Bacterial degradation of xenobiotic compounds: evolution and distribution of novel enzyme activities. Environ. Microbiol. 2005, 7, 1868-1882.
18. Janssen, D., Biocatalysis by dehalogenating enzymes. Adv. Appl. Microbiol. 2007, 61, 233-252.
19. Scott, C., Pandey, G., Hartley, C. J., Jackson, C. J. et al., The enzymatic basis for pesticide bioremediation. Indian J. Microbiol. 2008, 48, 65-79.
20. Gray, K. A., Richardson, T. H., Robertson, D. E., Swanson, P. E., Subramanian, M. V., Soil-based gene discovery: a new technology to accelerate and broaden biocatalytic applications. Adv. Appl. Microbiol. 2003, 52, 1-27.
21. Johri, A. K., Dua, M., Tuteja, D., Saxena, R. et al., Genetic manipulations of microorganisms for the degradation of hexachlorocyclohexane. FEMS Microbiol. Rev. 1996, 19, 69-84.
22. Kumar, S., Mukerji, K., Lal, R., Molecular aspects of pesticide degradation by microorganisms. Crit. Rev. Microbiol. 1996, 22, 1-26.
23. Lal, R., Dadhwal, M., Kumari, K., Sharma, P. et al., Pseudomonas sp. to Sphingobium indicum: a journey of microbial degradation and bioremediation of hexachlorocyclohexane. Indian J. Microbiol. 2008, 48, 3-18.
24. Lal, R., Pandey, G., Sharma, P., Kumari, K. et al., Biochemistry of microbial degradation of hexachlorocyclohexane and prospects for bioremediation. Microbiol. Mol. Biol. Rev. 2010, 74, 58-80.
25. Damborsky, J., Chaloupkova, R., Pavlova, M., Chovancova, E., Brezovsky, J., Structure-function relationships and engineering of haloalkane dehalogenases, in: Timmis, K. N. (Ed.), Handbook of Hydrocarbon and Lipid Microbiology, Springer, Berlin, Heidelberg 2010, pp. 1081-1098.
26. Keuning, S., Janssen, D. B., Witholt, B., Purification and characterization of hydrolytic haloalkane dehalogenase from Xanthobacter autotrophicus GJ10. J. Bacteriol. 1985, 163, 635-639.
27. Yokota, T., Omori, T., Kodama, T., Purification and properties of haloalkane dehalogenase from Corynebacterium sp. strain m15-3. J. Bacteriol. 1987, 169, 4049-4054.
28. Nagata, Y., Miyauchi, K., Damborsky, J., Manova, K. et al., Purification and characterization of a haloalkane dehalogenase of a new substrate class from a gamma-hexachlorocyclohexane-degrading bacterium, Sphingomonas paucimobilis UT26. Appl. Environ. Microbiol. 1997, 63, 3707-3710.
29. Jesenska, A., Bartos, M., Czernekova, V., Rychlik, I. et al., Cloning and expression of the haloalkane dehalogenase gene dhmA from Mycobacterium avium N85 and preliminary characterization of DhmA. Appl. Environ. Microbiol. 2002, 68, 3724-3730.
30. Jesenska, A., Pavlova, M., Strouhal, M., Chaloupkova, R. et al., Cloning, biochemical properties, and distribution of mycobacterial haloalkane dehalogenases. Appl. Environ. Microbiol. 2005, 71, 6736-6745.
31. Sato, Y., Monincova, M., Chaloupkova, R., Prokop, Z. et al., Two rhizobial strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, encode haloalkane dehalogenases with novel structures and substrate specificities. Appl. Environ. Microbiol. 2005, 71, 4372-4379.
32. Pavlova, M., Klvana, M., Jesenska, A., Prokop, Z. et al., The identification of catalytic pentad in the haloalkane dehalogenase DhmA from Mycobacterium avium N85: reaction mechanism and molecular evolution. J. Struct. Biol. 2007, 157, 384-392.
33. Jesenska, A., Monincova, M., Koudelakova, T., Hasan, K. et al., Biochemical characterization of haloalkane dehalogenases DrbA and DmbC, representatives of a novel subfamily. Appl. Environ. Microbiol. 2009, 75, 5157-5160.
34. Chan, W. Y., Wong, M., Guthrie, J., Savchenko, A. V. et al., Sequence- and activity-based screening of microbial genomes for novel dehalogenases. Microb. Biotechnol. 2010, 3, 107-120.
35. Hasan, K., Fortova, A., Koudelakova, T., Chaloupkova, R. et al., Biochemical characteristics of the novel haloalkane dehalogenase DatA, isolated from the plant pathogen Agrobacterium tumefaciens C58. Appl. Environ. Microbiol. 2011, 77, 1881-1884.
36. Hesseler, M., Bogdanovic, X., Hidalgo, A., Berenguer, J. et al., Cloning, functional expression, biochemical characterization, and structural analysis of a haloalkane dehalogenase from Plesiocystis pacifica SIR-1. Appl. Microbiol. Biotechnol. 2011, 91, 1049-1060.
37. Gehret, J. J., Gu, L., Geders, T. W., Brown, W. C. et al., Structure and activity of DmmA, a marine haloalkane dehalogenase. Protein Sci. 2012, 21, 239-248.
38. Drienovska, I., Chovancova, E., Koudelakova, T., Damborsky, J., Chaloupkova, R., Biochemical characterization of a novel haloalkane dehalogenase from a cold-adapted bacterium. Appl. Environ. Microbiol. 2012, 78, 4995-4998.
39. Janssen, D. B., Pries, F., Van Der Ploeg, J., Kazemier, B. et al., Cloning of 1, 2-dichloroethane degradation genes of Xanthobacter autotrophicus GJ10 and expression and sequencing of the dhlA gene. J. Bacteriol. 1989, 171, 6791-6799.
40. Nagata, Y., Natsui, S., Endo, R., Ohtsubo, Y. et al., Genomic organization and genomic structural rearrangements of Sphingobium japonicum UT26, an archetypal γ-hexachlorocyclohexane-degrading bacterium. Enzyme Microb. Tech. 2011, 49, 499-508.
41. Curragh, H., Flynn, O., Larkin, M. J., Stafford, T. M. et al., Haloalkane degradation and assimilation by Rhodococcus rhodochrous NCIMB 13064. Microbiology 1994, 140, 1433-1442.
42. Kulakova, A. N., Larkin, M. J., Kulakov, L. A., The plasmid-located haloalkane dehalogenase gene from Rhodococcus rhodochrous NCIMB 13064. Microbiology 1997, 109-115.
43. Poelarends, G. J., Kulakov, L. A., Larkin, M. J., Van Hylckama Vlieg, J. E., Janssen, D. B., Roles of horizontal gene transfer and gene integration in evolution of 1, 3-dichloropropene- and 1, 2-dibromoethane-degradative pathways. J. Bacteriol. 2000, 182, 2191-2199.
44. Prokop, Z., Oplustil, F., De Frank, J., Damborsky, J., Enzymes fight chemical weapons. Biotechnol. J. 2006, 1, 1370-1380.
45. Prokop, Z., Sato, Y., Brezovsky, J., Mozga, T. et al., Enantioselectivity of haloalkane dehalogenases and its modulation by surface loop engineering. Angew. Chem. Int. Ed. Engl. 2010, 49, 6111-6115.
46. Koudelakova, T., Chovancova, E., Brezovsky, J., Monincova, M. et al., Substrate specificity of haloalkane dehalogenases. Biochem. J. 2011, 435, 345-354.
47. Westerbeek, A., Szymanski, W., Wijma, H. J., Marrink, S. J. et al., Kinetic resolution of alpha-bromoamides: experimental and theoretical investigation of highly enantioselective reactions catalyzed by haloalkane dehalogenases. Adv. Synth. Catal. 2011, 353, 931-944.
48. Schanstra, J. P., Kingma, J., Janssen, D. B., Specificity and kinetics of haloalkane dehalogenase. J. Biol. Chem. 1996, 271, 14747-14753.
49. Bosma, T., Pikkemaat, M. G., Kingma, J., Dijk, J., Janssen, D. B., Steady-state and pre-steady-state kinetic analysis of halopropane conversion by a Rhodococcus haloalkane dehalogenase. Biochemistry 2003, 42, 8047-8053.
50. Schindler, J. F., Naranjo, P. A., Honaberger, D. A., Chang, C. H. et al., Haloalkane dehalogenases: steady-state kinetics and halide inhibition. Biochemistry 1999, 38, 5772-5778.
51. Kmunicek, J., Hynkova, K., Jedlicka, T., Nagata, Y. et al., Quantitative analysis of substrate specificity of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26. Biochemistry 2005, 44, 3390-3401.
52. Pavlova, M., Klvana, M., Prokop, Z., Chaloupkova, R. et al., Redesigning dehalogenase access tunnels as a strategy for degrading an anthropogenic substrate. Nat. Chem. Biol. 2009, 5, 727-733.
53. Chaloupkova, R., Sykorova, J., Prokop, Z., Jesenska, A. et al., Modification of activity and specificity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by engineering of its entrance tunnel. J. Biol. Chem. 2003, 278, 52622-52628.
54. Bar-Even, A., Noor, E., Savir, Y., Liebermeister, W. et al., The moderately efficient enzyme: evolutionary and physicochemical trends shaping enzyme parameters. Biochemistry 2011, 50, 4402-4410.
55. Janssen, D. B., Gerritse, J., Brackman, J., Kalk, C. et al., Purification and characterization of a bacterial dehalogenase with activity toward halogenated alkanes, alcohols and ethers. Eur. J. Biochem. 1988, 171, 67-72.
56. Pieters, R. J., Lutje Spelberg, J. H., Kellogg, R. M., Janssen, D. B., The enantioselectivity of haloalkane dehalogenases. Tetrahedron Lett. 2001, 42, 469-471.
57. Prokop, Z., Damborsky, J., Janssen, D. B., Nagata, Y., Method of production of optically active halohydrocarbons and alcohols using hydrolytic dehalogenation catalysed by haloalkane dehalogenases. US Patent 7632666, 2009.
58. Chaloupkova, R., Prokop, Z., Sato, Y., Nagata, Y., Damborsky, J., Stereoselectivity and conformational stability of haloalkane dehalogenase DbjA from Bradyrhizobium japonicum USDA110: the effect of pH and temperature. FEBS J. 2011, 278, 2728-2738.
59. Patel, R. N., Biocatalysis: synthesis of chiral intermediates for pharmaceuticals. Curr. Org. Chem. 2006, 10, 1289-1321.
60. Biedermann, J., Leon-Lomeli, A., Borbe, H. O., Prop, G., Two stereoisomeric imidazoline derivatives. Synthesis, optical, and alpha 2-adrenoceptor activities. J. Med. Chem. 1986, 29, 1183-1188.
61. Szymanski, W., Westerbeek, A., Janssen, D. B., Feringa, B. L., A simple enantioconvergent and chemoenzymatic synthesis of optically active alpha-substituted amides. Angew. Chem. Int. Ed. Engl. 2011, 50, 10712-10715.
62. Luetz, S., Giver, L., Lalonde, J., Engineered enzymes for chemical production. Biotechnol. Bioeng. 2008, 101, 647-653.
63. Westerbeek, A., Szymanski, W., Feringa, B. L., Janssen, D. B., Dynamic kinetic resolution process employing haloalkane dehalogenase. ACS Catal. 2011, 1, 1654-1660.
64. Tufvesson, P., Lima-Ramos, J., Nordblad, M., Woodley, J. M., Guidelines and cost analysis for catalyst production in biocatalytic processes. Org. Process Res. Dev. 2011, 15, 266-274.
65. Cheetham, P., What makes a good biocatalyst? J. Biotechnol. 1998, 66, 3-10.
66. Swanson, P. E., Method for conversion of halogenated hydrocarbons to halohydrins. US Patent 5372944, 1994.
67. Dravis, B., Swanson, P., Russell, A., Haloalkane hydrolysis with an immobilized haloalkane dehalogenase. Biotechnol. Bioeng. 2001, 75, 416-423.
68. Gray, K., Richardson, T., Kretz, K., Short, J. et al., Rapid evolution of reversible denaturation and elevated melting temperature in a microbial haloalkane dehalogenase. Adv. Synth. Catal. 2001, 343, 607-617.
69. Bosma, T., Damborsky, J., Stucki, G., Janssen, D., Biodegradation of 1, 2, 3-trichloropropane through directed evolution and heterologous expression of a haloalkane dehalogenase gene. Appl. Environ. Microbiol. 2002, 68, 3582-3587.
70. Zhao, H., A pH-indicator-based screen for hydrolytic haloalkane dehalogenase, in: Arnold, F. H., Georgiou, G. (Eds.), Directed Enzyme Evolution: Screening and Selection Methods, Humana Press, New Jersey, 2003, pp. 213-222.
71. Banas, P., Otyepka, M., Jerabek, P., Petrek, M., Damborsky, J., Mechanism of enhanced conversion of 1, 2, 3-trichloropropane by mutant haloalkane dehalogenase revealed by molecular modeling. J. Comput. Aided Mol. Des. 2006, 20, 375-383.
72. Klvana, M., Pavlova, M., Koudelakova, T., Chaloupkova, R. et al., Pathways and mechanisms for product release in the engineered haloalkane dehalogenases explored using classical and random acceleration molecular dynamics simulations. J. Mol. Biol. 2009, 392, 1339-1356.
73. Van Leeuwen, J. G. E., Wijma, H. J., Floor, R. J., Van Der Laan, J.-M., Janssen, D. B., Directed evolution strategies for enantiocomplementary haloalkane dehalogenases: from chemical waste to enantiopure building blocks. ChemBioChem 2012, 13, 137-148.
74. Kretz, K. A., Richardson, T. H., Gray, K. A., Robertson, D. E. et al., Gene site saturation mutagenesis: a comprehensive mutagenesis approach. Meth. Enzymol. 2004, 388, 3-11.
75. Mena-Benitez, G. L., Gandia-Herrero, F., Graham, S., Larson, T. R. et al., Engineering a catabolic pathway in plants for the degradation of 1, 2-dichloroethane. Plant Physiol. 2008, 147, 1192-1198.
76. Stucki, G., Thuer, M., Experiences of a large-scale application of 1, 2-dichloroethane degrading microorganisms for groundwater treatment. Environ. Sci. Technol. 1995, 29, 2339-2345.
77. Freitas dos Santos, L. M., Livingston, A. G., Novel membrane bioreactor for detoxification of VOC wastewaters: biodegradation of 1, 2-dichloroethane. Water Res. 1995, 29, 179-194.
78. Van Den Wijngaard, A. J., Janssen, D. B., Witholt, B., Degradation of epichlorohydrin and halohydrins by bacterial cultures isolated from freshwater sediment. J. Gen. Microbiol. 1989, 135, 2199-2208.
79. Bosma, T., Kruizinga, E., De Bruin, E. J., Poelarends, G. J., Janssen, D. B., Utilization of trihalogenated propanes by Agrobacterium radiobacter AD1 through heterologous expression of the haloalkane dehalogenase from Rhodococcus sp. strain M15-3. Appl. Environ. Microbiol. 1999, 65, 4575-4581.
80. Erable, B., Goubet, I., Lamare, S., Seltana, A. et al., Nonconventional hydrolytic dehalogenation of 1-chlorobutane by dehydrated bacteria in a continuous solid-gas biofilter. Biotechnol. Bioeng. 2005, 91, 304-313.
81. Erable, B., Maugard, T., Goubet, I., Lamare, S., Legoy, M. D., Biotransformation of halogenated compounds by lyophilized cells of Rhodococcus erythropolis in a continuous solid-gas biofilter. Process Biochem. 2005, 40, 45-51.
82. Erable, B., Goubet, I., Lamare, S., Legoy, M. D., Maugard, T., Haloalkane hydrolysis by Rhodococcus erythropolis cells: comparison of conventional aqueous phase dehalogenation and nonconventional gas phase dehalogenation. Biotechnol. Bioeng. 2004, 86, 47-54.
83. Erable, B., Goubet, I., Seltana, A., Maugard, T., Non-conventional gas phase remediation of volatile halogenated compounds by dehydrated bacteria. J. Environ. Manage. 2009, 90, 2841-2844.
84. Bala, K., Geueke, B., Miska, M. E., Rentsch, D. et al., Enzymatic conversion of ε{lunate}-hexachlorocyclohexane and a heptachlorocyclohexane isomer, two neglected components of technical hexachlorocyclohexane. Environ. Sci. Technol. 2012, 46, 4051-4058.
85. Heeb, N. V., Zindel, D., Geueke, B., Kohler, H.-P. E., Lienemann, P., Biotransformation of hexabromocyclododecanes (HBCDs) with LinB-an HCH-converting bacterial enzyme. Environ. Sci. Technol. 2012, 46, 6566-6574.
86. Naested, H., Fennema, M., Hao, L., Andersen, M. et al., A bacterial haloalkane dehalogenase gene as a negative selectable marker in Arabidopsis. Plant J. 1999, 18, 571-576.
87. Uchida, E., Ouchi, T., Suzuki, Y., Yoshida, T. et al., Secretion of bacterial xenobiotic-degrading enzymes from transgenic plants by an apoplastic expressional system: an applicability for phytoremediation. Environ. Sci. Technol. 2005, 39, 7671-7677.
88. Jez, J. M., Toward protein engineering for phytoremediation: possibilities and challenges. Int. J. Phytoremediation 2011, 13, 77-89.
89. Prokop, Z., Damborsky, J., Oplustil, F., Jesenska, A., Nagata, Y., Method of detoxication of yperite by using haloalkane dehalogenases. US Patent 7888103, 2011.
90. Alamo-Bethencourt, V., Aldridge, S., Coombs, A., DeFrancesco, L., Huggett, B., Osborne, R., Mustard gas enzyme, news in brief. Nat. Biotech. 2007, 25, 1197-1198.
91. Blum, M.-M., Richardt, A., in: Richardt A., Blum, M.-M. (Eds.), Decontamination of Warfare Agents, Wiley-VCH Verlag, Weinheim, 2008, pp. 135-162.
92. Peter, J., Hutter, W., Stöllnberger, W., Hampel, W., Detection of chlorinated and brominated hydrocarbons by an ion sensitive whole cell biosensor. Biosens. Bioelectron. 1996, 11, 1215-1219.
93. Campbell, D., Müller, C., Reardon, K., Development of a fiber optic enzymatic biosensor for 1, 2-dichloroethane. Biotechnol. Lett. 2006, 28, 883-887.
94. Reardon, K. F., Campbell, D. W., Müller, C., Optical fiber enzymatic biosensor for reagentless measurement of ethylene dibromide. Eng. Life Sci. 2009, 9, 291-297.
95. Bidmanova, S., Chaloupkova, R., Damborsky, J., Prokop, Z., Development of an enzymatic fiber-optic biosensor for detection of halogenated hydrocarbons. Anal. Bioanal. Chem. 2010, 398, 1891-1898.
96. Hutter, W., Peter, J., Swoboda, H., Hampel, W. et al., Development of a microbial bioassay for chlorinated and brominated hydrocarbons. Anal. Chim. Acta 1995, 306, 237-241.
97. Peter, J., Hutter, W., Stöllnberger, W., Karner, F., Hampel, W., Semicontinuous detection of 1, 2-dichloroethane in water samples using Xanthobacter autotrophicus GJ10 encapsulated in chitosan beads. Anal. Chem. 1997, 69, 2077-2079.
98. Bidmanova, S., Hlavacek, A., Damborsky, J., Prokop, Z., Conjugation of 5(6)-carboxyfluorescein and 5(6)-carboxynaphthofluorescein with bovine serum albumin and their immobilization for optical pH sensing. Sens. Actuators. B Chem. 2012, 161, 93-99.
99. Johnson, A. K., Zawadzka, A. M., Deobald, L. A., Crawford, R. L., Paszczynski, A. J., Novel method for immobilization of enzymes to magnetic nanoparticles. J. Nanopart. Res. 2008, 10, 1009-1025.
100. Jordana, S., Piera, E. B., Natural groundwater quality and health. Geol. Acta 2004, 2, 175-188.
101. Scheidleder, A., Grath, J., Winkler, G., Stärk, U. et al., Groundwater quality and quantity in Europe, Office for Official Publications of the European Communities, Copenhagen, 1999, pp. 78-82.
102. Los, G. V., Darzins, A., Karassina, N., Zimprich, C. et al., HaloTag interchangeable labeling technology for cell imaging and protein capture. Cell Notes 2005, 11, 2-6.
103. Los, G., Learish, R., Karassina, N., Zimprich, C. et al., HaloTag technology: cell imaging and protein analysis. Cell Notes 2006, 14, 10-14.
104. Los, G. V., Wood, K., The HaloTag: a novel technology for cell imaging and protein analysis. Methods Mol. Biol. 2007, 356, 195-208.
105. Los, G., Encell, L., McDougall, M., Hartzell, D. et al., HaloTag: A novel protein labeling technology for cell imaging and protein analysis. ACS Chem. Biol. 2008, 3, 373-382.
106. Darzins, A., Encell, L., Los, G. V., Wood, K. V. et al., Covalent tethering of functional groups to proteins and substrates therefor. US Patent 7425436, 2008.
107. Ohana, R. F., Encell, L. P., Zhao, K., Simpson, D. et al., HaloTag7: a genetically engineered tag that enhances bacterial expression of soluble proteins and improves protein purification. Protein Expr. Purif. 2009, 68, 110-120.
108. Mendez, J. L., Ohana, R. F., Hurst, R., Murphy, N. et al., Highly efficient protein and complex purification from mammalian cells using the HaloTag technology. Biotechniques 2011, 51, 276-277.
109. Ohana, R. F., Hurst, R., Vidugiriene, J., Slater, M. R. et al., HaloTag-based purification of functional human kinases from mammalian cells. Protein Expr. Purif. 2011, 76, 154-164.
110. Leippe, D. M., Zhao, K. Q., Hsiao, K., Slater, M. R., Cell-free expression of protein kinase a for rapid activity assays. Anal. Chem. Insights 2010, 5, 25-36.
111. Nath, N., Hurst, R., Hook, B., Meisenheimer, P. et al., Improving protein array performance: focus on washing and storage conditions. J. Proteome Res. 2008, 7, 4475-4482.
112. Urh, M., Hartzell, D., Mendez, J., Klaubert, D. H., Wood, K., Methods for detection of protein-protein and protein-DNA interactions using HaloTag. Methods Mol. Biol. 2008, 421, 191-209.
113. Hartzell, D. D., Trinklein, N. D., Mendez, J., Murphy, N. et al., A functional analysis of the CREB signaling pathway using HaloCHIP-chip and high throughput reporter assays. BMC Genomics 2009, 10.
114. Hurst, R., Hook, B., Slater, M. R., Hartnett, J. et al., Protein-protein interaction studies on protein arrays: Effect of detection strategies on signal-to-background ratios. Anal. Biochem. 2009, 392, 45-53.
115. Daniels, D. L., Mendez, J., Mosley, A. L., Ramisetty, S. R. et al., Examining the complexity of human RNA polymerase complexes using HaloTag technology coupled to label free quantitative proteomics. J. Proteome Res. 2012, 11, 564-575.
116. Darzins, A., Encell, L., Johnson, T., Klaubert, D. et al., Method of immobilizing a protein or molecule via a mutant dehalogenase that is bound to an immobilized dehalogenase substrate and linked directly or indirectly to the protein or molecule. US Patent 7888086, 2011.
117. Wood, K. V., Klaubert, D., Los, G. V., Bulleit, R. F. et al., Covalent tethering of functional groups to proteins. US Patent RE42931, 2011.
118. Wood, K. V., Klaubert, D., Los, G. V., Bulleit, R. F. et al., Compositions comprising a dehalogenase substrate and a fluorescent label and methods of use. US Patent 7867726, 2011.
119. Sallis, P. J., Armfield, S. J., Bull, A. T., Hardman, D. J., Isolation and characterization of a haloalkane halidohydrolase from Rhodococcus erythropolis Y2. J. Gen. Microbiol. 1990, 136, 115-120.
120. Newman, J., Peat, T. S., Richard, R., Kan, L. et al., Haloalkane dehalogenases: structure of a Rhodococcus enzyme. Biochemistry 1999, 38, 16105-16114.
121. Liu, X., Hanson, B. L., Langan, P., Viola, R. E., The effect of deuteration on protein structure: a high-resolution comparison of hydrogenous and perdeuterated haloalkane dehalogenase. Acta Crystallogr. D Biol. Crystallogr. 2007, 63, 1000-1008.
122. Mazumdar, P. A., Hulecki, J. C., Cherney, M. M., Garen, C. R., James, M. N. G., X-ray crystal structure of Mycobacterium tuberculosis haloalkane dehalogenase Rv2579. Biochim. Biophys. Acta 2008, 1784, 351-362.
123. Oakley, A. J., Klvana, M., Otyepka, M., Nagata, Y. et al., Crystal structure of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26 at 0.95 Å resolution: dynamics of catalytic residues. Biochemistry 2004, 43, 870-878.
124. Gasteiger, E., Gattiker, A., Hoogland, C., Ivanyi, I. et al., ExPASy: the proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res. 2003, 31, 3784-3788.
125. Jesenska, A., Sykora, J., Olzynska, A., Brezovsky, J. et al., Nanosecond time-dependent Stokes shift at the tunnel mouth of haloalkane dehalogenases. J. Am. Chem. Soc. 2009, 131, 494-501.