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Volumn 87, Issue 4, 2011, Pages 846-852

Quantum yields and quantitative spectra of firefly bioluminescence with various bivalent metal ions

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CATION; FIREFLY LUCIFERASE; INSECT PROTEIN; LUCIFERIN; METAL;

EID: 79960559914     PISSN: 00318655     EISSN: 17511097     Source Type: Journal    
DOI: 10.1111/j.1751-1097.2011.00931.x     Document Type: Article
Times cited : (36)

References (21)
  • 1
    • 2442437836 scopus 로고    scopus 로고
    • Biotechnological applications of bioluminescence and chemiluminescence
    • DOI 10.1016/j.tibtech.2004.03.011, PII S016777990400085X
    • Roda, A., P. Pasini, M. Mirasoli, E. Michelini, and, M. Guardigli, (2004) Biotechnological applications of bioluminescence and chemiluminescence. Trends Biotechnol. 22, 295-303. (Pubitemid 38639777)
    • (2004) Trends in Biotechnology , vol.22 , Issue.6 , pp. 295-303
    • Roda, A.1    Pasini, P.2    Mirasoli, M.3    Michelini, E.4    Guardigli, M.5
  • 2
    • 0002468820 scopus 로고
    • The colors of firefly bioluminescence: Enzyme configuration and species specificity
    • Seliger, H. H., and, W. D. McElroy, (1964) The colors of firefly bioluminescence: Enzyme configuration and species specificity. Proc. Natl Acad. Sci. USA 52, 75-81.
    • (1964) Proc. Natl Acad. Sci. USA , vol.52 , pp. 75-81
    • Seliger, H.H.1    McElroy, W.D.2
  • 3
    • 0014498808 scopus 로고
    • The spectroscopic properties of firefly luciferin and related compounds. An approach to product emission
    • Morton, R. A., T. A. Hopkins, and, H. H. Seliger, (1969) The spectroscopic properties of firefly luciferin and related compounds. An approach to product emission. Biochemistry 8 (4), 1598-1607.
    • (1969) Biochemistry , vol.8 , Issue.4 , pp. 1598-1607
    • Morton, R.A.1    Hopkins, T.A.2    Seliger, H.H.3
  • 4
    • 0014873578 scopus 로고
    • Substrate-binding properties of firefly luciferase II. ATP-binding site
    • Lee, R. T., J. L. Denburg, and, W. D. McElroy, (1970) Substrate-binding properties of firefly luciferase II. ATP-binding site. Arch. Biochem. Biophys. 141, 38-52.
    • (1970) Arch. Biochem. Biophys. , vol.141 , pp. 38-52
    • Lee, R.T.1    Denburg, J.L.2    McElroy, W.D.3
  • 5
    • 0000372063 scopus 로고
    • Spectral emission and quantum yield of firefly bioluminescence
    • Seliger, H. H., and, W. D. McElroy, (1960) Spectral emission and quantum yield of firefly bioluminescence. Arch. Biochem. Biophys. 88, 136-141.
    • (1960) Arch. Biochem. Biophys. , vol.88 , pp. 136-141
    • Seliger, H.H.1    McElroy, W.D.2
  • 8
    • 0032858233 scopus 로고    scopus 로고
    • Site-directed mutagenesis of firefly luciferase active site amino acids: A proposed model for bioluminescence color
    • Branchini, B. R., R. A. Magyar, M. H. Murtiashaw, S. M. Anderson, L. C. Helgerson, and, M. Zimmer, (1999) Site-directed mutagenesis of firefly luciferase active site amino acids: A proposed model for bioluminescence color. Biochemistry 38 (40), 13223-13230.
    • (1999) Biochemistry , vol.38 , Issue.40 , pp. 13223-13230
    • Branchini, B.R.1    Magyar, R.A.2    Murtiashaw, M.H.3    Anderson, S.M.4    Helgerson, L.C.5    Zimmer, M.6
  • 9
    • 34548747539 scopus 로고    scopus 로고
    • Development of a quantitative bio/chemiluminescence spectrometer determining quantum yields: Re-examination of the aqueous luminol chemiluminescence standard
    • DOI 10.1111/j.1751-1097.2007.00140.x
    • Ando, Y., K. Niwa, N. Yamada, T. Irie, T. Enomoto, H. Kubota, Y. Ohmiya, and, H. Akiyama, (2007) Development of a quantitative bio/chemiluminescence spectrometer determining quantum yields: Re-examination of the aqueous luminol chemiluminescence standard. Photochem. Photobiol. 83 (5), 1205-1210. (Pubitemid 47438519)
    • (2007) Photochemistry and Photobiology , vol.83 , Issue.5 , pp. 1205-1210
    • Ando, Y.1    Niwa, K.2    Yamada, N.3    Irie, T.4    Enomoto, T.5    Kubota, H.6    Ohmiya, Y.7    Akiyama, H.8
  • 11
    • 0242421530 scopus 로고
    • Stereospecificity and firefly bioluminescence, a comparison of natural and synthetic luciferins
    • Seliger, H. H., W. D. McElroy, E. H. White, and, G. F. Field, (1961) Stereospecificity and firefly bioluminescence, a comparison of natural and synthetic luciferins. Proc. Natl Acad. Sci. USA 47, 1129-1134.
    • (1961) Proc. Natl Acad. Sci. USA , vol.47 , pp. 1129-1134
    • Seliger, H.H.1    McElroy, W.D.2    White, E.H.3    Field, G.F.4
  • 12
    • 0023665984 scopus 로고
    • Kinetic effects of ATP, divalent metal ions and pH on chicken liver mevalonate 5-diphosphate decarboxylase
    • Jabalquinto, A. M., and, E. Cardemil, (1987) Kinetic effects of ATP, divalent metal ions and pH on chicken liver mevalonate 5-diphosphate decarboxylase. Biochim. Biophys. Acta 916, 172-178.
    • (1987) Biochim. Biophys. Acta , vol.916 , pp. 172-178
    • Jabalquinto, A.M.1    Cardemil, E.2
  • 14
    • 0031042173 scopus 로고    scopus 로고
    • Mutagenesis of firefly luciferase shows that cysteine residues are not required for bioluminescence activity
    • DOI 10.1016/S0014-5793(97)00105-1, PII S0014579397001051
    • Ohmiya, Y., and, F. I. Tsuji, (1997) Mutagenesis of firefly luciferase shows that cysteine residues are not required for bioluminescence activity. FEBS Lett. 404, 115-117. (Pubitemid 27113435)
    • (1997) FEBS Letters , vol.404 , Issue.2-3 , pp. 115-117
    • Ohmiya, Y.1    Tsuji, F.I.2
  • 15
    • 0011220868 scopus 로고
    • Role of sulfhydryl groups in firefly luciferase
    • DeLuca, M., G. W. Wirtz, and, W. D. McElroy, (1964) Role of sulfhydryl groups in firefly luciferase. Biochemistry 3, 935-939.
    • (1964) Biochemistry , vol.3 , pp. 935-939
    • Deluca, M.1    Wirtz, G.W.2    McElroy, W.D.3
  • 16
    • 0018565112 scopus 로고
    • Inhibition of glutathione peroxidase by cadmium and other metal ions
    • DOI 10.1016/0003-9861(79)90277-7
    • Splittgerber, A. G., and, A. L. Tappel, (1979) Inhibition of glutathione peroxidase by cadmium and other metal ions. Arch. Biochem. Biophys. 197, 534-542. (Pubitemid 10200644)
    • (1979) Archives of Biochemistry and Biophysics , vol.197 , Issue.2 , pp. 534-542
    • Splittgerber, A.G.1    Tappel, A.L.2
  • 17
    • 0032518199 scopus 로고    scopus 로고
    • Inhibition of NF-κB binding to DNA by chromium, cadmium, mercury, zinc, and arsenite in vitro: Evidence of a thiol mechanism
    • DOI 10.1006/abbi.1997.0470
    • Shumilla, J. A., K. E. Wetterhahn, and, A. Barchowsky, (1998) Inhibition of NF-kappaB binding to DNA by chromium, cadmium, mercury, zinc, and arsenite in vitro: Evidence of a thiol mechanism. Arch. Biochem. Biophys. 349, 356-362. (Pubitemid 28368681)
    • (1998) Archives of Biochemistry and Biophysics , vol.349 , Issue.2 , pp. 356-362
    • Shumilla, J.A.1    Wetterhahn, K.E.2    Barchowsky, A.3
  • 18
    • 0038063472 scopus 로고
    • The interaction of cadmium and zinc ions with thiol-substituted dextrans
    • Gaber, B. P., and, A. L. Fluharty, (1971) The interaction of cadmium and zinc ions with thiol-substituted dextrans. Bioinorg. Chem. 1, 65-78.
    • (1971) Bioinorg. Chem. , vol.1 , pp. 65-78
    • Gaber, B.P.1    Fluharty, A.L.2
  • 19
    • 0019877634 scopus 로고
    • Regulation of rat liver carbamyl phosphate synthetase I. Inhibition by metal ions and activation by amino acids and other chelating agents
    • Powers, S. G., (1981) Regulation of rat liver carbamyl phosphate synthetase I. Inhibition by metal ions and activation by amino acids and other chelating agents. J. Bio. Chem. 256, 11160-11165.
    • (1981) J. Bio. Chem. , vol.256 , pp. 11160-11165
    • Powers, S.G.1
  • 20
    • 0028798434 scopus 로고
    • Oxidative mechanisms in the toxicity of metal ions
    • Stohs, S. J., and, D. Bagchi, (1995) Oxidative mechanisms in the toxicity of metal ions. Free Radic. Biol. Med. 18, 321-336.
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 321-336
    • Stohs, S.J.1    Bagchi, D.2
  • 21
    • 0030584662 scopus 로고    scopus 로고
    • Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes
    • Conti, E., N. P. Franks, and, P. Brick, (1996) Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure 4, 287-298.
    • (1996) Structure , vol.4 , pp. 287-298
    • Conti, E.1    Franks, N.P.2    Brick, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.