Sequence-alignment modelling and molecular docking studies of the epoxygenase component of alkene monooxygenase from Nocardia corallina B-276

European Journal of Biochemistry

Volumn 254, Issue 3, 1998, Pages 480-489

  Gallagher, Stephen C ^a   George, Ashley ^b   Dalton, Howard ^a  

^a UNIVERSITY OF WARWICK   (United Kingdom)

^b GLAXOSMITHKLINE   (United Kingdom)

Author keywords

Diiron; Epoxide; Molecular docking; Monooxygenase; Stereoselective

Indexed keywords

OXYGENASE;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ASSAY; ENZYME ISOLATION; ENZYME SUBSTRATE COMPLEX; NOCARDIA; NONHUMAN; PRIORITY JOURNAL; SEQUENCE ANALYSIS; STEREOCHEMISTRY;

AMINO ACID SEQUENCE; BINDING SITES; DIAZONIUM COMPOUNDS; DIETHYL PYROCARBONATE; IRON; LIGANDS; MOLECULAR SEQUENCE DATA; NOCARDIA; OXYGENASES; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); CORALLINA; GORDONIA RUBRIPERTINCTUS; NOCARDIA;

EID: 0032526267     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2540480.x     Document Type: Article

References (24)

1. Nordlund, P., Dalton, H. & Eklund, H. (1992) The active site structure of methane monooxygenase is closely related to the binuclear iron center of ribonucleotide reductase, FEBS Lett. 307, 257-262.
2. Rosenzweig, A. C., Frederick, C. A., Lippard, S. J. & Nordlund, P. (1993) Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane, Nature 366, 537-543.
3. Rosenzweig, A. C, Nordlund, P., Takahara, P., Frederick, C. A. & Lippard, S. J.(1995) Geometry of the soluble methane monooxygenase catalytic diiron centre in two oxidation states, Chem. & Biol. 2, 409-418.
4. George, A. R., Wilkins, P. C. & Dalton, H. (1996) A computational investigation of the possible substrate binding sites in the hydroxylase of soluble methane monooxygenase, J. Mol. Catal. 2, 103-113.
5. Saeki, H. & Furuhashi, K. (1994) Cloning and characterisation of a Nocardia corallina B-276 gene cluster encoding alkene monooxygenase, J. Ferment. Bioeng. 78, 399-406.
6. Gallagher, S. C., Cammack, R. & Dalton, H. (1997) Alkene monooxygenase from Nocardia corallina B-276 is a member of the class of dinuclear iron proteins capable of stereospecific epoxygenation reactions, Eur. J. Biochem. 247, 635-641.
7. Green, J. & Dalton, H. (1988) The biosynthesis and assembly of protein A of soluble methane monooxygenase of Methylococcus capsulatus (Bath), J. Biol. Chem. 263, 17561-17565.
8. Miura, A. & Dalton, H. (1995) Purification and characterisation of the alkene monooxygenase from Nocardia corallina B-276, Biosci. Biotech. Biochem. 59, 853-859.
9. Smith, D. D. S. & Dalton, H. (1992) Evidence for two histidine ligands at the diiron site of methane monooxygenase, Eur. J. Biochem. 210, 629-633.
10. Wilcox, P. (1972) Esterification, Methods Enzymol. 25, 596-615.
11. Miller, R. T., Jones, D. T. & Thornton, J. M. (1996) Protein fold recognition by sequence threading-tools and assessment techniques, FASEB J. 10, 171-178.
12. Sali, A. & Blundell, T. L. (1993) Comparative protein modelling by satisfaction of spatial restraints, J. Mol. Biol. 234, 779-815.
13. Leach, A. (1996) Molecular modelling principles and applications, Longman Press, London.
14. Bradford, M. M. (1976) A rapid and sensitive method for the detection of microgram quantities of protein utilising the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
15. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
16. Wilkins, P. C. & Dalton, H. (1994) Variations on a theme of Fe-O-Fe proteins, Biochem. Soc. Trans. 22, 700-704.
17. Campbell, I. D. & Dwek, R. A. (1984) Biological spectroscopy, Benjamin/Cummings Publishing Co. Inc., California.
18. Elango, N., Radharishnan, R., Froland, W. A., Wallar, B. J., Earhart, C. A., Lipscomb, J. D. & Ohlendorf, D. H. (1997) Crystal structure of the hydroxylase component of methane monooxygenase from Methylosinus trichosporium OB3b, Prot. Sci. 6, 556-568.
19. Nordlund, P., Sjoberg, B. M. & Eklund, H. (1990) Three dimensional structure of the free radical protein of ribonucleotide reductase, Nature 345, 593-598.
20. Green, J. & Dalton, H. (1989) Substrate specificity of soluble methane monooxygenase (mechanistic implications), J. Biol. Chem. 264, 17698-17703.
21. Fox, B. G., Borneman, J. G., Wackett, L. P. & Lipscomb, J. D. (1990) Haloalkane oxidation by the soluble methane monooxygenase from Methylosinus trichosporium OB3b - mechanistic and environmental implications, Biochemistry 29, 6419-6427.
22. Dalton, H., Smith, D. D. S. & Pilkington, S. J. (1990) Towards a unified mechanism of biological methane oxidation, FEMS Microbiol. Rev. 87, 201-208.
23. Jiang, Y., Wilkins, P. C. & Dalton, H. (1993) Activation of the hydroxylase of soluble MMO from Methylococcus capsulatus (Bath) by hydrogen peroxide, Biochim. Biophys. Acta 1163, 105-112.
24. Liu, K. & Lippard, S. J. (1995) Redox properties of the hydroxylase of methane monooxygenase from Methylococcus capsulatus (Bath), J. Am. Chem. Soc. 117, 4987-4990.