Stopped-flow spectrophotometric and resonance Raman analyses of aldoxime dehydratase involved in carbon-nitrogen triple bond synthesis

FEBS Letters

Volumn 579, Issue 6, 2005, Pages 1394-1398

  Oinuma, Ken Ichi ^a   Kumita, Hideyuki ^b   Ohta, Takehiro ^c   Konishi, Kazunobu ^a   Hashimoto, Yoshiteru ^a   Higashibata, Hiroki ^a   Kitagawa, Teizo ^c   Shiro, Yoshitsugu ^b   Kobayashi, Michihiko ^a  

^a UNIVERSITY OF TSUKUBA   (Japan)

^b RIKEN HARIMA INSTITUTE   (Japan)

^c NATIONAL INSTITUTES OF NATURAL SCIENCES   (Japan)

Author keywords

Dehydration; Heme; Nitrile; Reaction intermediate; Resonance Raman spectroscopy; Stopped flow spectrophotometry

Indexed keywords

ALDOXIME; ALDOXIME DEHYDRATASE; ALIPHATIC COMPOUND; CARBON; FERROUS ION; HEME; HEMOPROTEIN; MUTANT PROTEIN; NITROGEN; UNCLASSIFIED DRUG;

ABSORPTION SPECTROSCOPY; ARTICLE; CHEMICAL BOND; FLOW MEASUREMENT; PRIORITY JOURNAL; RAMAN SPECTROMETRY; SYNTHESIS;

EID: 14244264537     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.01.037     Document Type: Article

References (40)

1. M. Kobayashi, and S. Shimizu Metalloenzyme nitrile hydratase: structure, regulation, and application to biotechnology Nature Biotechnol. 16 1998 733 736
2. H. Komeda, M. Kobayashi, and S. Shimizu A novel gene cluster including the Rhodococcus rhodochrous J1 nhlBA genes encoding a low molecular mass nitrile hydratase (L-NHase) induced by its reaction product J. Biol. Chem. 271 1996 15796 15802
3. H. Komeda, M. Kobayashi, and S. Shimizu Characterization of the gene cluster of high-molecular-mass nitrile hydratase (H-NHase) induced by its reaction product in Rhodococcus rhodochrous J1 Proc. Natl. Acad. Sci. USA 93 1996 4267 4272
4. M. Kobayashi, H. Komeda, N. Yanaka, T. Nagasawa, and H. Yamada Nitrilase from Rhodococcus rhodochrous J1. Sequencing and overexpression of the gene and identification of an essential cysteine residue J. Biol. Chem. 267 1992 20746 20751
5. M. Goda, Y. Hashimoto, S. Shimizu, and M. Kobayashi Discovery of a novel enzyme, isonitrile hydratase, involved in nitrogen-carbon triple bond cleavage J. Biol. Chem. 276 2001 23480 23485
6. M. Goda, Y. Hashimoto, M. Takase, S. Herai, Y. Iwahara, H. Higashibata, and M. Kobayashi Isonitrile hydratase from Pseudomonas putida N19-2. Cloning, sequencing, gene expression, and identification of its active acid residue J. Biol. Chem. 277 2002 45860 45865
7. H. Fukatsu, Y. Hashimoto, M. Goda, H. Higashibata, and M. Kobayashi Amine-synthesizing enzyme N-substituted formamide deformylase: screening, purification, characterization, and gene cloning Proc. Natl. Acad. Sci. USA 101 2004 13726 13731
8. M. Kobayashi, T. Nagasawa, and H. Yamada Enzymatic synthesis of acrylamide: a success story not yet over Trends Biotechnol. 10 1992 402 408
9. H. Yamada, and M. Kobayashi Nitrile hydratase and its application to industrial production of acrylamide Biosci. Biotechnol. Biochem. 60 1996 1391 1400
10. M. Kobayashi, N. Yanaka, T. Nagasawa, and H. Yamada Primary structure of an aliphatic nitrile-degrading enzyme, aliphatic nitrilase, from Rhodococcus rhodochrous K22 and expression of its gene and identification of its active site residue Biochemistry 31 1992 9000 9007
11. H. Komeda, Y. Hori, M. Kobayashi, and S. Shimizu Transcriptional regulation of the Rhodococcus rhodochrous J1 nitA gene encoding a nitrilase Proc. Natl. Acad. Sci. USA 93 1996 10572 10577
12. M. Kobayashi, H. Izui, T. Nagasawa, and H. Yamada Nitrilase in biosynthesis of the plant hormone indole-3-acetic acid from indole-3- acetonitrile: cloning of the Alcaligenes gene and site-directed mutagenesis of cysteine residues Proc. Natl. Acad. Sci. USA 90 1993 247 251
13. M. Kobayashi, T. Suzuki, T. Fujita, M. Masuda, and S. Shimizu Occurrence of enzymes involved in biosynthesis of indole-3-acetic acid from indole-3-acetonitrile in plant-associated bacteria, Agrobacterium and Rhizobium Proc. Natl. Acad. Sci. USA 92 1995 714 718
14. M. Kobayashi, and S. Shimizu Cobalt proteins Eur. J. Biochem. 261 1999 1 9
15. Y. Asano, Y. Tani, and H. Yamada A new enzyme, nitrile hydratase, which degrades acetonitrile in combination with amidase Agric. Biol. Chem. 44 1980 2251 2252
16. V.C. Popescu, E. Munck, B.G. Fox, Y. Sanakis, J.G. Cummings, I.M. Turner Jr., and M.J. Nelson Mössbauer and EPR studies of the photoactivation of nitrile hydratase Biochemistry 40 2001 7984 7991
17. M. Kobayashi, Y. Fujiwara, M. Goda, H. Komeda, and S. Shimizu Identification of active sites in amidase: evolutionary relationship between amide bond- and peptide bond-cleaving enzymes Proc. Natl. Acad. Sci. USA 94 1997 11986 11991
18. M. Kobayashi, M. Goda, and S. Shimizu The catalytic mechanism of amidase also involves nitrile hydrolysis FEBS Lett. 439 1998 325 328
19. M. Kobayashi, H. Komeda, T. Nagasawa, M. Nishiyama, S. Horinouchi, T. Beppu, H. Yamada, and S. Shimizu Amidase coupled with low-molecular-mass nitrile hydratase from Rhodococcus rhodochrous J1. Sequencing and expression of the gene and purification and characterization of the gene product Eur. J. Biochem. 217 1993 327 336
20. H. Yamada, S. Shimizu, and M. Kobayashi Hydratases involved in nitrile conversion: screening, characterization and application Chemical Records 1 2001 152 161
21. I. Endo, M. Odaka, and M. Yohda An enzyme controlled by light: the molecular mechanism of photoreactivity in nitrile hydratase Trends Biotechnol. 17 1999 244 248
22. T. Nagasawa, H. Nanba, K. Ryuno, K. Takeuchi, and H. Yamada Nitrile hydratase of Pseudomonas chlororaphis B23. Purification and characterization Eur. J. Biochem. 162 1987 691 698
23. T. Nagasawa, K. Ryuno, and H. Yamada Superiority of Pseudomonas chlororaphis B23 nitrile hydratase as a catalyst for the enzymatic production of acrylamide Experiential 45 1989 1066 1070
24. E.G. Hann, A. Eisenberg, S.K. Fager, N.E. Perkins, F.G. Gallagher, S.M. Cooper, J.E. Gavagan, B. Stieglitz, S.M. Hennessey, and R. DiCosimo 5-Cyanovaleramide production using immobilized Pseudomonas chlororaphis B23 Bioorg. Med. Chem. 7 1999 2239 2245
25. K.-I. Oinuma, Y. Hashimoto, K. Konishi, M. Goda, T. Noguchi, H. Higashibata, and M. Kobayashi Novel aldoxime dehydratase involved in carbon-nitrogen triple bond synthesis of Pseudomonas chlororaphis B23. Sequencing, gene expression, purification, and characterization J. Biol. Chem. 278 2003 29600 29608
26. M. Nishiyama, S. Horinouchi, M. Kobayashi, T. Nagasawa, H. Yamada, and T. Beppu Cloning and characterization of genes responsible for metabolism of nitrile compounds from Pseudomonas chlororaphis B23 J. Bacteriol. 173 1991 2465 2472
27. Available from: 〈http://www.chem.qmul.ac.uk/iubmb/enzyme/EC4/99/1/5. html〉
28. Y. Kato, K. Nakamura, H. Sakiyama, S.G. Mayhew, and Y. Asano Novel heme-containing lyase, phenylacetaldoxime dehydratase from Bacillus sp. strain OxB-1: purification, characterization, and molecular cloning of the gene Biochemistry 39 2000 800 809
29. S.-X. Xie, Y. Kato, H. Komeda, S. Yoshida, and Y. Asano A gene cluster responsible for alkylaldoxime metabolism coexisting with nitrile hydratase and amidase in Rhodococcus globerulus A-4 Biochemistry 42 2003 12056 12066
30. S.-X. Xie, Y. Kato, and Y. Asano High yield synthesis of nitriles by a new enzyme, phenylacetaldoxime dehydratase, from Bacillus sp. strain OxB-1 Biosci. Biotechnol. Biochem. 65 2001 2666 2672
31. K.-I. Oinuma, T. Ohta, K. Konishi, Y. Hashimoto, H. Higashibata, T. Kitagawa, and M. Kobayashi Heme environment in aldoxime dehydratase involved in carbon-nitrogen triple bond synthesis FEBS Lett. 568 2004 44 48
32. K. Konishi, K. Ishida, K.-I. Oinuma, T. Ohta, Y. Hashimoto, H. Higashibata, T. Kitagawa, and M. Kobayashi Identification of crucial histidines involved in carbon-nitrogen triple bond synthesis by aldoxime dehydratase J. Biol. Chem. 279 2004 47619 47625
33. J. Hart-Davis, P. Battioni, J.-L. Boucher, and D. Mansuy New catalytic properties of iron porphyrins: model systems for cytochrome P450-catalyzed dehydration of aldoximes J. Am. Chem. Soc. 120 1998 12524 12530
34. J.-L. Boucher, M. Delaforge, and D. Mansuy Dehydration of alkyl- and arylaldoximes as a new cytochrome P450-catalyzed reaction: mechanism and stereochemical characteristics Biochemistry 33 1994 7811 7818
35. V.M. Guzov, H.L. Houston, M.B. Murataliev, F.A. Walker, and R. Feyereisen Molecular cloning, overexpression in Escherichia coli, structural and functional characterization of house fly cytochrome b5 J. Biol. Chem. 271 1996 26637 26645
36. D. Shelver, R.L. Kerby, Y. He, and G.P. Roberts CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein Proc. Natl. Acad. Sci. USA 94 1997 11216 11220
37. T.G. Spiro, and X.-Y. Li Resonance Raman spectroscopy of metalloporphyrins T.G. Spiro Biological Applications of Raman Spectroscopy vol. III 1988 Wiley New York 1 37
38. T. Kitagawa, Y. Kyogoku, T. Iizuka, M. Ikeda-Saito, and T. Yamanaka Resonance Raman scattering from hemoproteins. Effects of ligands upon the Raman spectra of various C-type cytochromes J. Biochem. 78 1975 719 728
39. T. Uchida, H. Ishikawa, S. Takahashi, K. Ishimori, I. Morishima, K. Ohkubo, H. Nakajima, and S. Aono Heme environmental structure of CooA is modulated by the target DNA binding. Evidence from resonance Raman spectroscopy and CO rebinding kinetics J. Biol. Chem. 273 1998 19988 19992
40. N. Parthasarathi, C. Hansen, S. Yamaguchi, and T.G. Spiro Metalloporphyrin core size resonance Raman marker bands revisited: implications for the interpretation of hemoglobin photoproduct Raman frequencies J. Am. Chem. Soc. 109 1987 3865 3871