Structural and functional analysis of bacterial flavin-containing monooxygenase reveals its ping-pong-type reaction mechanism

Journal of Structural Biology

Volumn 175, Issue 1, 2011, Pages 39-48

  Cho, Hyo Je ^a   Cho, Ha Yeon ^a   Kim, Kyung Jin ^b   Kim, Myung Hee ^c   Kim, Si Wouk ^d   Kang, Beom Sik ^a  

^a Kyungpook National University   (South Korea)

^b POSTECH   (South Korea)

^c Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

^d Chosun University   (South Korea)

Author keywords

Flavin containing monooxygenase; Indole oxygenation; Ping pong reaction; Protein structure

Indexed keywords

ARGININE; FLAVINE ADENINE NUCLEOTIDE; INDOLE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; TYROSINE; UNSPECIFIC MONOOXYGENASE;

ARTICLE; BINDING SITE; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; OXYGENATION; PRIORITY JOURNAL; REACTION ANALYSIS;

AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BINDING SITES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ENZYME ASSAYS; ENZYME INHIBITORS; INDOLES; MUTAGENESIS, SITE-DIRECTED; NADP; OXYGENASES; PISCIRICKETTSIACEAE; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS;

BACTERIA (MICROORGANISMS);

EID: 79956190420     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2011.04.007     Document Type: Article

References (26)

1. Alfieri A., Malito E., Orru R., Fraaije M.W., Mattevi A. Revealing the moonlighting role of NADP in the structure of a flavin-containing monooxygenase. Proc. Natl. Acad. Sci. USA 2008, 105:6572-6577.
2. Beaty N.B., Ballou D.P. The reductive half-reaction of liver microsomal FAD-containing monooxygenase. J. Biol. Chem. 1981, 256:4611-4618.
3. Beaty N.B., Ballou D.P. The oxidative half-reaction of liver microsomal FAD-containing monooxygenase. J. Biol. Chem. 1981, 256:4619-4625.
4. Berman H.M., Henrick K., Nakamura H. Announcing the worldwide Protein Data Bank. Nat. Struc. Biol. 2003, 10:980.
5. Choi H.S., Kim J.K., Cho E.H., Kim Y.C., Kim J.I., Kim S.W. A novel flavin-containing monooxygenase from Methylophaga sp. strain SK1 and its indigo synthesis in Escherichia coli. Biochem. Biophys. Res. Commun. 2003, 306:930-936.
6. Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 2004, 60:2126-2132.
7. Ensley B.D., Ratzkin B.J., Osslund T.D., Simon M.J., Wackett L.P., Gibson D.T. Expression of naphthalene oxidation genes in Escherichia coli results in the biosynthesis of indigo. Science 1983, 222:167-169.
8. Entsch B., van Berkel W.J.H. Structure and mechanism of para-hydroxybenzoate hydroxylase. FASEB J. 1995, 9:476-483.
9. Eswaramoorthy S., Bonanno J.B., Burley S.K., Swaminathan S. Mechanism of action of a flavin-containing monooxygenase. Proc. Natl. Acad. Sci. USA 2006, 103:9832-9837.
10. Fraaije M.W., Kamerbeek N.M., van Berkel W.J.H., Janssen D.B. Identification of a Baeyer-Villiger monooxygenase sequence motif. FEBS Lett. 2002, 518:43-47.
11. Kamerbeek N.M., Fraaije M.W., Janssen D.B. Identifying determinants of NADPH specificity in Baeyer-Villiger monooxygenase. Eur. J. Biochem. 2004, 271:2107-2116.
12. Krueger S.K., Williams D.E. Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism. Pharmacol. Ther. 2005, 106:357-387.
13. Kwon N.R., Chae J., Choi K.Y., Yoo M., Zylstra G.J., Kim Y.M., Kang B.S., Kim E. Identification of functionally important amino acids in a novel indigo-producing oxygenase from Phodococcus sp. strain T104. Appl. Microbiol. Biotechnol. 2008, 79:417-422.
14. Malito E., Alfieri A., Fraaije M.W., Mattevi A. Crystal structure of a Baeyer-Villiger monooxygenase. Proc. Natl. Acad. Sci. USA 2004, 101:13157-13162.
15. Massey V. Activation of molecular oxygen by flavins and flavoproteins. J. Biol. Chem. 1994, 269:22459-22462.
16. Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 1997, 53:240-255.
17. Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 1997, 276:307-326.
18. Suh J.K., Poulsen L.L., Ziegler D.M., Robertus J.D. Yeast flavin-containing monooxygenase generates oxidizing equivalents that control protein folding in the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 1999, 96:2687-2691.
19. Terwilliger T.C. Maximum-likelihood density modification. Acta Crystallogr. D 2000, 56:965-972.
20. Terwilliger T.C., Berendzen J. Automated MAD and MIR structure solution. Acta Crystallogr. D 1999, 55:849-861.
21. Vagin A., Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Cryst. 1997, 30:1022-1025.
22. van Berkel W.J.H., Kamerbeek N.M., Fraaije M.W. Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts. J. Biotechnol. 2006, 124:670-689.
23. Woo H., Sanseverino J., Cox C.D., Robinson K.G., Sayler G.S. The measurement of toluene dioxygenase activity in biofilm culture of Pseudomonas putida F1. J. Microbiol. Methods 2000, 40:181-191.
24. Zhao Y., Christensen S.K., Fankhauser C., Cashman J.R., Cohen J.D., Weigel D., Chory J. A role for flavin monooxygenase-like enzymes in auxin biosynthesis. Science 2001, 291:306-309.
25. Zhou J., Shephard E.A. Mutation, polymorphism and perspectives for the future of human flavin-containing monooxygenase 3. Mutat. Res. 2006, 612:165-171.
26. Ziegler D.M., Poulsen L.L. Hepatic microsomal mixed-function amine oxidase. Methods Enzymol. 1978, 52:142-151.