The flavin monooxygenases

Handbook of Flavoproteins: Complex Flavoproteins, Dehydrogenases and Physical Methods

Volumn 2, Issue , 2013, Pages 51-72

  Montersino, Stefania ^a   van Berkel, Willem J H ^b  

^a Wageningen University ^*

^b WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84979164600     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1515/9783110298345.51     Document Type: Chapter

References (119)

1. Torres Pazmino DE, Winkler M, Glieder A, Fraaije MW. Monooxygenases as biocatalysts: classification, mechanistic aspects and biotechnological applications. J Biotechnol 2010;146:9-24.
2. Fetzner S, Steiner RA. Cofactor-independent oxidases and oxygenases. Appl Microbiol Biotechnol 2010;86:791-804.
3. Fisher AJ, Raushel FM, Baldwin TO, Rayment I. Three-dimensional structure of bacterial luci-ferase from Vibrio harveyi at 2.4 A resolution. Biochemistry 1995;34:6581-6.
4. Harwood CS, Parales RE. The beta-ketoadipate pathway and the biology of self-identity. Ann Rev Microbiol 1996;50:553-90.
5. Phale PS, Basu A, Majhi PD, Deveryshetty J, Vamsee-Krishna C, Shrivastava R. Metabolic diversity in bacterial degradation of aromatic compounds. Omics 2007;11:252-79.
6. Ahmad M, Roberts JN, Hardiman EM, Singh R, Eltis LD, Bugg TDH. Identification of DypB from Rhodococcus jostii RHA1 as a lignin peroxidase. Biochemistry 2011;50:5096-107.
7. Kallio P, Liu Z, Mäntsälä P, Niemi J, Metsä-Ketelä M. Sequential action of two flavoenzymes, PgaE and PgaM, in angucycline biosynthesis: chemoenzymatic synthesis of gaudimycin C. Chem Biol 2008;15:157-66.
8. Lindqvist Y, Koskiniemi H, Jansson A, Sandalova T, Schnell R, Liu Z, Mäntsälä P, Niemi J, Schneider G. Structural basis for substrate recognition and specificity in aklavinone-11-hydroxylase from rhodomycin biosynthesis. J Mol Biol 2009;393:966-77.
9. Ryan KS, Howard-Jones AR, Hamill MJ, Elliott SJ, Walsh CT, Drennan CL. Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC. Proc Natl Acad Sci USA 2007;104:15311-6.
10. Olucha J, Lamb AL. Mechanistic and structural studies of the N-hydroxylating flavoprotein monooxygenases. Bioorg Chem 2011;39:171-7.
11. Schlaich NL. Flavin-containing monooxygenases in plants: looking beyond detox. Trends Plant Sci 2007;12:412-8.
12. Siebold C, Berrow N, Walter TS, Owens RJ, Stuart DI, Terman JR, Kolodkin AL, Pasterkamp RJ, Jones EY. High-resolution structure of the catalytic region of MICAL (molecule interacting with CasL), a multidomain flavoenzyme-signaling molecule. Proc Natl Acad Sci USA 2005;102:16836-41.
13. Hung RJ, Yazdani U, Yoon J, Wu H, Yang T, Gupta N, Huang Z, van Berkel WJ, Terman JR. Mical links semaphorins to F-actin disassembly. Nature 2010;463:823-7.
14. Palfey BA, McDonald CA. Control of catalysis in flavin-dependent monooxygenases. Arch Biochem Biophys 2010;493:26-36.
15. Vervoort J, Muller F, Lee J, Vandenberg WAM, Moonen CTW. Identifications of the True C-13 Nuclear-Magnetic-Resonance Spectrum of the Stable Intermediate-Ii in Bacterial Luciferase. Biochemistry 1986;25:8062-7.
16. van Berkel WJH, Kamerbeek NM, Fraaije MW. Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts. J Biotechnol 2006;124:670-89.
17. Ghisla S, Massey V. Mechanisms of flavoprotein-catalyzed reactions. Eur J Biochem 1989;181:1-17.
18. Massey V. Activation of molecular oxygen by flavins and flavoproteins. J Biol Chem 1994;269:22459-62.
19. Baron R, McCammon JA, Mattevi A. The oxygen-binding vs. oxygen-consuming paradigm in biocatalysis: structural biology and biomolecular simulation. Curr Opin Struct Biol 2009;19:672-9.
20. Chaiyen P, Fraaije MW, Mattevi A. The enigmatic reaction of flavins with oxygen. Trends Biochem Sci 2012;37:373-80.
21. Entsch B, van Berkel WJH. Structure and mechanism of para-hydroxybenzoate hydroxylase. FASEB J 1995;9:476-83.
22. Chen L, Lyubimov AY, Brammer L, Vrielink A, Sampson NS. The binding and release of oxygen and hydrogen peroxide are directed by a hydrophobic tunnel in cholesterol oxidase. Biochemistry 2008;47:5368-77.
23. Baron R, Riley C, Chenprakhon P, Thotsaporn K, Winter RT, Alfieri A, Forneris F, van Berkel WJH, Chaiyen P, Fraaije MW, Mattevi A, McCammon JA. Multiple pathways guide oxygen diffusion into flavoenzyme active sites. Proc Natl Acad Sci USA 2009;106:10603-8.
24. Kommoju P-R, Chen Z-w, Bruckner RC, Mathews FS, Jorns MS. Probing oxygen activation sites in two flavoprotein oxidases using chloride as an oxygen surrogate. Biochemistry 2011;50:5521-34.
25. Wierenga RK, de Jong RJ, Kalk KH, Hol WG, Drenth J. Crystal structure of p-hydroxybenzoate hydroxylase. J Mol Biol 1979;131:55-73.
26. Montersino S, Tischler D, Gassner GT, van Berkel WJH. Catalytic and structural features of flavoprotein hydroxylases and epoxidases. Adv Synth Catal 2011;353:2301-19.
27. Chaiyen P. Flavoenzymes catalyzing oxidative aromatic ring-cleavage reactions. Arch Bio-chem Biophys 2010;493:62-70.
28. Malito E, Alfieri A, Fraaije MW, Mattevi A. Crystal structure of a Baeyer-Villiger monooxygenase. Proc Natl Acad Sci USA 2004;101:13157-62.
29. Torres Pazmino DE, Dudek HM, Fraaije MW. Baeyer-Villiger monooxygenases: recent advances and future challenges. Curr Opin Chem Biol 2010;14:138-44.
30. Walsh CT, Chen YCJ. Enzymic Baeyer-Villiger oxidations by flavin-dependent monooxygenases. Angew Chem 1988;27:333-43.
31. Taylor DG, Trudgill PW. Camphor revisited: studies of 2,5-diketocamphane 1,2-monooxygenase from Pseudomonas putida ATCC 17453. J Bacteriol 1986;165:489-97.
32. Eichhorn E, Davey CA, Sargent DF, Leisinger T, Richmond TJ. Crystal structure of Escherichia coli alkanesulfonate monooxygenase SsuD. J Mol Biol 2002;324:457-68.
33. Valton J, Fontecave M, Douki T, Kendrew SG, Niviere V. An aromatic hydroxylation reaction catalyzed by a two-component FMN-dependent monooxygenase. The ActVA-ActVB system from Streptomyces coelicolor. J Biol Chem 2006;281:27-35.
34. Chaiyen P, Suadee C, Wilairat P. A novel two-protein component flavoprotein hydroxylase. Eur J Biochem 2001;268:5550-61.
35. Ukaegbu UE, Kantz A, Beaton M, Gassner GT, Rosenzweig AC. Structure and ligand binding properties of the epoxidase component of styrene monooxygenase. Biochemistry 2010;49:1678-88.
36. Tischler D, Eulberg D, Lakner S, Kaschabek SR, van Berkel WJH, Schlömann M. Identification of a novel self-sufficient styrene monooxygenase from Rhodococcus opacus 1CP. J Bacteriol 2009;191:4996-5009.
37. Dong C, Flecks S, Unversucht S, Haupt C, van Pee K-H, Naismith JH. Tryptophan 7-halo-genase (PrnA) structure suggests a mechanism for regioselective chlorination. Science 2005;309:2216-9.
38. Jeffers CE, Nichols JC, Tu SC. Complex formation between Vibrio harveyi luciferase and monomeric NADPH:FMN oxidoreductase. Biochemistry 2003;42:529-34.
39. Ellis HR. The FMN-dependent two-component monooxygenase systems. Arch Biochem Bio-phys 2010;497:1-12.
40. Valton J, Filisetti L, Fontecave M, Niviere V. A two-component flavin-dependent monooxygenase involved in actinorhodin biosynthesis in Streptomyces coelicolor. J Biol Chem 2004;279:44362-9.
41. Chung HW, Tu SC. Structure-function relationship of Vibrio harveyi NADPH-flavin oxidoreductase FRP: essential residues Lys167 and Arg15 for NADPH binding. Biochemistry 2012;51:4880-7.
42. Kirchner U, Westphal AH, Muller R, van Berkel WJ. Phenol hydroxylase from Bacillus ther-moglucosidasius A7, a two-protein component monooxygenase with a dual role for FAD. J Biol Chem 2003;278:47545-53.
43. van den Heuvel RH, Westphal AH, Heck AJ, Walsh MA, Rovida S, van Berkel WJ, Mattevi A. Structural studies on flavin reductase PheA2 reveal binding of NAD in an unusual folded conformation and support novel mechanism of action. J Biol Chem 2004;279:12860-7.
44. van Lanen SG, Lin S, Horsman GP, Shen B. Characterization of SgcE6, the flavin reductase component supporting FAD-dependent halogenation and hydroxylation in the biosynthesis of the enediyne antitumor antibiotic C-1027. FEMS Microbiol Lett 2009;300:237-41.
45. Ludwig ML, Andersen RD, Mayhew SG, Massey V. The structure of a clostridial flavodoxin. I. Crystallographic characterization of the oxidized and semiquinone forms. J Biol Chem 1969;244:6047-8.
46. Schulz GE, Schirmer RH, Sachsenheimer W, Pai EF. The structure of the flavoenzyme glutathione reductase. Nature 1978;273:120-4.
47. Macheroux P, Kappes B, Ealick SE. Flavogenomics--a genomic and structural view of flavin-dependent proteins. FEBS J 2011;278:2625-34.
48. Wierenga RK, Terpstra P, Hol WG. Prediction of the occurrence of the ADP-binding beta alpha beta-fold in proteins, using an amino acid sequence fingerprint. J Mol Biol 1986;187:101-7.
49. Rossmann MG, Moras D, Olsen KW. Chemical and biological evolution of nucleotide-binding protein. Nature 1974;250:194-9.
50. Eggink G, Engel H, Vriend G, Terpstra P, Witholt B. Rubredoxin reductase of Pseudomonas oleovorans. Structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints. J Mol Biol 1990;212:135-42.
51. Eppink MHM, van Berkel WJH, Schreuder HA. Identification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD/NAD(P)H binding. Protein Sci 1997;6:2454-8.
52. Fraaije MW, Kamerbeek NM, van Berkel WJH, Janssen DB. Identification of a Baeyer-Villiger monooxygenase sequence motif. FEBS Lett 2002;518:43-7.
53. Riebel A, Dudek HM, de Gonzalo G, Stepniak P, Rychlewski L, Fraaije MW. Expanding the set of rhodococcal Baeyer-Villiger monooxygenases by high-throughput cloning, expression and substrate screening. Appl Microbiol Biotechnol 2012;95:1479-89.
54. Fraaije MW, Wu J, Heuts DP, van Hellemond EW, Spelberg JH, Janssen DB. Discovery of a thermostable Baeyer-Villiger monooxygenase by genome mining. Appl Microbiol Biotechnol 2005;66:393-400.
55. Montersino S, van Berkel WJH. Functional annotation and characterization of 3-hydroxyben-zoate 6-hydroxylase from Rhodococcus jostii RHA1. Biochim Biophys Acta 2012;1824:433-42.
56. McLeod MP, Warren RL, Hsiao WWL, Araki N, Myhre M, Fernandes C, Miyazawa D, Wong W, Lillquist AL, Wang D, Dosanjh M, Hara H, Petrescu A, Morin RD, Yang G, Stott JM, Schein JE, Shin H, Smailus D, Siddiqui AS, Marra MA, Jones SJM, Holt R, Brinkman FSL, Miyauchi K, Fukuda M, Davies JE, Mohn WW, Eltis LD. The complete genome of Rhodococcus sp. RHA1 provides insights into a catabolic powerhouse. Proc Natl Acad Sci USA 2006;103:15582-7.
57. Galán B, Diaz E, Prieto MA, Garcia JL. Functional analysis of the small component of the 4-hydroxyphenylacetate 3-monooxygenase of Escherichia coliW: a prototype of a new flavin: NAD(P)H reductase subfamily. J Bacteriol 2000;182:627-36.
58. Flecks S, Patallo EP, Zhu X, Ernyei AJ, Seifert G, Schneider A, Dong C, Naismith JH, van Pée K-H. New insights into the mechanism of enzymatic chlorination of tryptophan. Angew Chem 2008;47:9533-6.
59. Hornung A, Bertazzo M, Dziarnowski A, Schneider K, Welzel K, Wohlert S-E, Holzenkämpfer M, Nicholson GJ, Bechthold A, Süssmuth RD, Vente A, Pelzer S. A genomic screening approach to the structure-guided identification of drug candidates from natural sources. Chem-BioChem 2007;8:757-66.
60. Tischler D, Gröning JAD, Kaschabek SR, Schlömann M. One-component styrene monooxygenases: an evolutionary view on a rare class of flavoproteins. Appl Biochem Biotechnol 2012;167:931-44.
61. Lin H, Qiao J, Liu Y, Wu ZL. Styrene monooxygenase from Pseudomonas sp. LQ26 catalyzes the asymmetric epoxidation of both conjugated and unconjugated alkenes. J Mol Catal B: Enzym 2010;67:236-41.
62. Marconi AM, Beltrametti F, Bestetti G, Solinas F, Ruzzi M, Galli E, Zennaro E. Cloning and characterization of styrene catabolism genes from Pseudomonas fluorescens ST. App Environ Microbiol 1996;62:121-7.
63. Mooney A, Ward PG, O'Connor KE. Microbial degradation of styrene: biochemistry, molecular genetics, and perspectives for biotechnological applications. Appl Microbiol Biotechnol 2006;72:1-10.
64. Panke S, Wubbolts MG, Schmid A, Witholt B. Production of enantiopure styrene oxide by recombinant Escherichia coli synthesizing a two-component styrene monooxygenase. Biotechnol Bioeng 2000;69:91-100.
65. Park MS, Bae JW, Han JH, Lee EY, Lee SG, Park S. Characterization of styrene catabolic genes of Pseudomonas putida SN1 and construction of a recombinant Escherichia coli containing styrene monooxygenase gene for the production of (S)-styrene oxide. J Microbiol Biotechnol 2006;16:1032-40.
66. van Hellemond EW, Janssen DB, Fraaije MW. Discovery of a novel styrene monooxygenase originating from the metagenome. App Environ Microbiol 2007;73:5832-9.
67. Tischler D, Kermer R, Gröning JAD, Kaschabek SR, van Berkel WJH, Schlömann M. StyAI and StyA2B from Rhodococcus opacus 1CP: a multifunctional styrene monooxygenase system. J Bacteriol 2010;192:5220-7.
68. van Berkel WJH, Müller F. Flavin-dependent monooxygenases with special reference to p-hydroxybenzoate hydroxylase. In: Müller F, ed. Chemistry and Biochemistry of Flavoenzymes, Vol II. Boca Raton: CRC Press USA; 1991:1-29.
69. Entsch B, Cole LJ, Ballou DP. Protein dynamics and electrostatics in the function of p-hydroxy-benzoate hydroxylase. Arch Biochem Biophys 2005;433:297-311.
70. Chaiyen P, Brissette P, Ballou DP, Massey V. Thermodynamics and reduction kinetics properties of 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase. Biochemistry 1997;36:2612-21.
71. Mohanty SK, Yu CL, Das S, Louie TM, Gakhar L, Subramanian M. Delineation of the caffeine C-8 oxidation pathway in Pseudomonas sp. strain CBB1 via characterization of a new trimethyluric acid monooxygenase and genes involved in trimethyluric acid metabolism. J Bacteriol 2012;194:3872-82.
72. Howard-Jones AR, Walsh CT. Staurosporine and rebeccamycin aglycones are assembled by the oxidative action of StaP, StaC, and RebC on chromopyrrolic acid. J Am Chem Soc 2006;128:12289-98.
73. Asamizu S, Shiro Y, Igarashi Y, Nagano S, Onaka H. Characterization and functional modification of StaC and RebC, which are involved in the pyrrole oxidation of indolocarbazole biosynthesis. Biosci Biotechnol Biochem 2011;75:2184-93.
74. Koskiniemi H, Metsä-Ketelä M, Dobritzsch D, Kallio P, Korhonen H, Mäntsälä P, Schneider G, Niemi J. Crystal structures of two aromatic hydroxylases involved in the early tailoring steps of angucycline biosynthesis. J Mol Biol 2007;372:633-48.
75. Volkers G, Palm GJ, Weiss MS, Wright GD, Hinrichs W. Structural basis for a new tetracycline resistance mechanism relying on the TetX monooxygenase. FEBS Lett 2011;585:1061-6.
76. Hiromoto T, Fujiwara S, Hosokawa K, Yamaguchi H. Crystal structure of 3-hydroxybenzoate hydroxylase from Comamonas testosteroni has a large tunnel for substrate and oxygen access to the active site. J Mol Biol 2006;364:878-96.
77. Eppink MHM, Boeren SA, Vervoort J, van Berkel WJH. Purification and properties of 4-hy-droxybenzoate 1-hydroxylase (decarboxylating), a novel flavin adenine dinucleotide-dependent monooxygenase from Candida parapsilosis CBS604. J Bacteriol 1997;179:6680-7.
78. Holesova Z, Jakubkova M, Zavadiakova I, Zeman I, Tomaska L, Nosek J. Gentisate and 3-oxoadi-pate pathways in the yeast Candida parapsilosis: identification and functional analysis of the genes coding for 3-hydroxybenzoate 6-hydroxylase and 4-hydroxybenzoate 1-hydroxylase. Microbiology 2011;157:2152-63.
79. Hartmann S, Hultschig C, Eisenreich W, Fuchs G, Bacher A, Ghisla S. NIH shift in flavin-dependent monooxygenation: mechanistic studies with 2-aminobenzoyl-CoA monooxygenase/reductase. Proc Natl Acad Sci USA 1999;96:7831-6.
80. Schühle K, Jahn M, Ghisla S, Fuchs G. Two similar gene clusters coding for enzymes of a new type of aerobic 2-aminobenzoate (anthranilate) metabolism in the bacterium Azoarcus evansii. J Bacteriol 2001;183:5268-78.
81. Ishiyama D, Vujaklija D, Davies J. Novel pathway of salicylate degradation by Streptomyces sp. strain WA46. App Environ Microbiol 2004;70:1297-306.
82. Giessen TW, Kraas FI, Marahiel MA. A four-enzyme pathway for 3,5-dihydroxy-4-meth-ylanthranilic acid formation and incorporation into the antitumor antibiotic sibiromycin. Biochemistry 2011;50:5680-92.
83. Ryerson CC, Ballou DP, Walsh C. Mechanistic studies on cyclohexanone oxygenase. Biochemistry 1982;21:2644-55.
84. Sheng D, Ballou DP, Massey V. Mechanistic studies of cyclohexanone monooxygenase: chemical properties of intermediates involved in catalysis. Biochemistry 2001;40:11156-67.
85. Mirza IA, Yachnin BJ, Wang S, Grosse S, Bergeron Hln, Imura A, Iwaki H, Hasegawa Y, Lau PCK, Berghuis AM. Crystal structures of cyclohexanone monooxygenase reveal complex domain movements and a sliding cofactor. J Am Chem Soc 2009;131:8848-54.
86. Kamerbeek NM, Moonen MJ, van der Ven JG, van Berkel WJH, Fraaije MW, Janssen DB. 4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB: a novel flavoprotein catalyzing Baeyer-Villiger oxidation of aromatic compounds. Eur J Biochem 2001;268:2547-57.
87. Orru R, Dudek HM, Martinoli C, Torres Pazmiño DE, Royant A, Weik M, Fraaije MW, Mattevi A. Snapshots of enzymatic Baeyer-Villiger catalysis: oxygen activation and intermediate stabilization. J Biol Chem 2011;286:29284-91.
88. Reetz MT, Wu S. Laboratory evolution of robust and enantioselective Baeyer-Villiger monooxygenases for asymmetric catalysis. J Am Chem Soc 2009;131:15424-32.
89. Wu S, Acevedo JP, Reetz MT. Induced allostery in the directed evolution of an enantioselective Baeyer-Villiger monooxygenase. Proc Natl Acad Sci USA 2010;107:2775-80.
90. Dudek HM, de Gonzalo G, Pazmiño DET, Stepniak P, Wyrwicz LS, Rychlewski L, Fraaije MW. Mapping the substrate binding site of phenylacetone monooxygenase from Thermobi-fida fusca by mutational analysis. App Environ Microbiol 2011;77:5730-8.
91. Franceschini S, van Beek HL, Pennetta A, Martinoli C, Fraaije MW, Mattevi A. Exploring the structural basis of substrate preferences in Baeyer-Villiger monooxygenases: insight from steroid monooxygenase. J Biol Chem 2012;287:22626-34.
92. Torres Pazmiño DE, Riebel A, de Lange J, Rudroff F, Mihovilovic MD, Fraaije MW. Efficient biooxidations catalyzed by a new generation of self-sufficient Baeyer-Villiger monooxygenases. ChemBioChem 2009;10:2595-8.
93. 2 addition but not flavin reduction. Biochemistry 2009;48:4371-6.
94. Mayfield JA, Frederick RE, Streit BR, Wencewicz TA, Ballou DP, DuBois JL. Comprehensive spectroscopic, steady state, and transient kinetic studies of a representative siderophore-associated flavin monooxygenase. J Biol Chem 2010;285:30375-88.
95. Olucha J, Meneely KM, Chilton AS, Lamb AL. Two structures of an N-hydroxylating flavoprotein monooxygenase: ornithine hydroxylase from Pseudomonas aeruginosa. J Biol Chem 2011;286:31789-98.
96. Robinson R, Sobrado P. Substrate binding modulates the activity of Mycobacterium smeg-matis G, a flavin-dependent monooxygenase involved in the biosynthesis of hydroxamate-containing siderophores. Biochemistry 2011;50:8489-96.
97. Al-Waiz M, Ayesh R, Mitchell SC, Idle JR, Smith RL. Trimethylaminuria (fish-odour syndrome): an inborn error of oxidative metabolism. Lancet 1987;1:634-5.
98. Dolphin CT, Janmohamed A, Smith RL, Shephard EA, Phillips IR. Missense mutation in flavin-containing mono-oxygenase 3 gene, FMO3, underlies fish-odour syndrome. Nat Genet 1997;17:491-4.
99. Orru R, Pazmino DET, Fraaije MW, Mattevi A. Joint functions of protein residues and NADP(H) in oxygen activation by flavin-containing monooxygenase. J Biol Chem 2010;285:35021-8.
100. Jensen CN, Cartwright J, Ward J, Hart S, Turkenburg JP, Ali ST, Allen MJ, Grogan G. A flavoprotein monooxygenase that catalyses a Baeyer-Villiger reaction and thioether oxidation using NADH as the nicotinamide cofactor. ChemBioChem 2012;13:872-8.
101. Eichhorn E, van der Ploeg JR, Leisinger T. Characterization of a two-component alkanesulfo-nate monooxygenase from Escherichia coli. J Biol Chem 1999;274:26639-46.
102. Ellis HR. Mechanism for sulfur acquisition by the alkanesulfonate monooxygenase system. Bioorg Chem 2011;39:178-84.
103. Li L, Liu X, Yang W, Xu F, Wang W, Feng L, Bartlam M, Wang L, Rao Z. Crystal structure of long-chain alkane monooxygenase (LadA) in complex with coenzyme FMN: unveiling the long-chain alkane hydroxylase. J Mol Biol 2008;376:453-65.
104. Mukherjee T, Zhang Y, Abdelwahed S, Ealick SE, Begley TP. Catalysis of a flavoenzyme-mediated amide hydrolysis. J Am Chem Soc 2010;132:5550-1.
105. Sucharitakul J, Phongsak T, Entsch B, Svasti J, Chaiyen P, Ballou DP. Kinetics of a two-component p-hydroxyphenylacetate hydroxylase explain how reduced flavin is transferred from the reductase to the oxygenase. Biochemistry 2007;46:8611-23.
106. Sucharitakul J, Chaiyen P, Entsch B, Ballou DP. The reductase of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii requires p-hydroxyphenylacetate for effective catalysis. Biochemistry 2005;44:10434-42.
107. Ruangchan N, Tongsook C, Sucharitakul J, Chaiyen P. pH-dependent studies reveal an efficient hydroxylation mechanism of the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase. J Biol Chem 2011;286:223-33.
108. Tongsook C, Sucharitakul J, Thotsaporn K, Chaiyen P. Interactions with the substrate phenolic group are essential for hydroxylation by the oxygenase component of p-hydroxyphenyl-acetate 3-hydroxylase. J Biol Chem 2011;286:44491-502.
109. Phongsak T, Sucharitakul J, Thotsaporn K, Oonanant W, Yuvaniyama J, Svasti J, Ballou DP, Chaiyen P. The C-terminal domain of 4-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii is an autoinhibitory domain. J Biol Chem 2012;287: 26213-22.
110. Uetz T, Schneider R, Snozzi M, Egli T. Purification and characterization of a two-component monooxygenase that hydroxylates nitrilotriacetate from "Chelatobacter" strain ATCC 29600. J Bacteriol 1992;174:1179-88.
111. Valton J, Mathevon C, Fontecave M, Niviere V, Ballou DP. Mechanism and regulation of the two-component FMN-dependent monooxygenase ActVA-ActVB from Streptomyces coeli-color. J Biol Chem 2008;283:10287-96.
112. Siitonen V, Blauenburg B, Kallio P, Mantsala P, Metsa-Ketela M. Discovery of a two-component monooxygenase SnoaW/SnoaL2 involved in nogalamycin biosynthesis. Chem Biol 2012;19:638-46.
113. Schmid A, Hofstetter K, Feiten HJ, Hollmann F, Witholt B. Integrated biocatalytic synthesis on gram scale: the highly enantioselective preparation of chiral oxiranes with styrene monooxygenase. Adv Synth Catal 2001;343:732-7.
114. Gursky LJ, Nikodinovic-Runic J, Feenstra KA, O'Connor KE. In vitro evolution of styrene monooxygenase from Pseudomonas putida CA-3 for improved epoxide synthesis. Appl Microbiol Biotechnol 2010;85:995-1004.
115. Qaed AA, Lin H, Tang D-F, Wu Z-L. Rational design of styrene monooxygenase mutants with altered substrate preference. Biotechnol Lett 2011;33:611-6.
116. Lin H, Tang DF, Ahmed AA, Liu Y, Wu ZL. Mutations at the putative active cavity of styrene monooxygenase: Enhanced activity and reversed enantioselectivity. J Biotechnol 2012.
117. van Pee K-H, Patallo EP. Flavin-dependent halogenases involved in secondary metabolism in bacteria. Appl Microbiol Biotechnol 2006;70:631-41.
118. Blasiak LC, Drennan CL. Structural perspective on enzymatic halogenation. Acc Chem Res 2009;42:147-55.
119. Buedenbender S, Rachid S, Muller R, Schulz GE. Structure and action of the myxobacterial chondrochloren halogenase CndH: a new variant of FAD-dependent halogenases. J Mol Biol 2009;385:520-30.