메뉴 건너뛰기




Volumn 121, Issue 3, 1997, Pages 477-486

In vitro assembly of FAD, AMP, and the two subunits of electron-transferring flavoprotein: An important role of AMP related with the conformational change of the apoprotein

Author keywords

AMP; Assembly; Conformation; Electron transferring flavoprotein; Subunit

Indexed keywords

ADENOSINE PHOSPHATE; APOPROTEIN; FLAVINE ADENINE NUCLEOTIDE; FLAVOPROTEIN;

EID: 0030897671     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021612     Document Type: Article
Times cited : (12)

References (21)
  • 1
    • 0001481670 scopus 로고
    • On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A: II. the electron-transferring flavoprotein
    • Crane, F.L. and Beinert, H. (1956) On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A: II. The electron-transferring flavoprotein. J. Biol. Chem. 218, 717-731
    • (1956) J. Biol. Chem. , vol.218 , pp. 717-731
    • Crane, F.L.1    Beinert, H.2
  • 2
    • 0141588541 scopus 로고
    • On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A: I. the general fatty acyl coenzyme A dehydrogenase
    • Crane, F.L., Mii, S., Hauge, J.G., Green, D.E., and Beinert, H. (1956) On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A: I. The general fatty acyl coenzyme A dehydrogenase. J. Biol. Chem. 218, 701-716
    • (1956) J. Biol. Chem. , vol.218 , pp. 701-716
    • Crane, F.L.1    Mii, S.2    Hauge, J.G.3    Green, D.E.4    Beinert, H.5
  • 3
    • 0019016567 scopus 로고
    • Isovaleryl-CoA dehydrogenase: Demonstration in rat liver mitochondria by ion exchange chromatography and isoelectric focusing
    • Noda, C., Rhead, W.J., and Tanaka, K. (1980) Isovaleryl-CoA dehydrogenase: Demonstration in rat liver mitochondria by ion exchange chromatography and isoelectric focusing. Proc. Natl. Acad. Sci. USA 77, 2646-2650
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2646-2650
    • Noda, C.1    Rhead, W.J.2    Tanaka, K.3
  • 4
    • 0021111556 scopus 로고
    • Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria
    • Ikeda, Y., Dabrowski, C., and Tanaka, K. (1983) Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria. J. Biol. Chem. 258, 1066-1067
    • (1983) J. Biol. Chem. , vol.258 , pp. 1066-1067
    • Ikeda, Y.1    Dabrowski, C.2    Tanaka, K.3
  • 5
    • 0017691203 scopus 로고
    • A new iron-sulfur flavoprotein of the respiratory chain: A component of the fatty acid β oxidation pathway
    • Ruzicka, F.J. and Beinert, H. (1977) A new iron-sulfur flavoprotein of the respiratory chain: A component of the fatty acid β oxidation pathway. J. Biol. Chem. 252, 8440-8445
    • (1977) J. Biol. Chem. , vol.252 , pp. 8440-8445
    • Ruzicka, F.J.1    Beinert, H.2
  • 6
    • 0027244216 scopus 로고
    • Electron-transferring flavoprotein has an AMP-binding site in addition to the FAD-binding site
    • Sato, K., Nishina, Y., and Shiga, K. (1993) Electron-transferring flavoprotein has an AMP-binding site in addition to the FAD-binding site. J. Biochem. 114, 215-222
    • (1993) J. Biochem. , vol.114 , pp. 215-222
    • Sato, K.1    Nishina, Y.2    Shiga, K.3
  • 7
    • 0028299835 scopus 로고
    • Electron-transferring flavoprotein from pig and the methylotrophic bacterium W3A1 contains AMP as well as FAD
    • DuPlessis, E.R., Rohlfs, R.J., Hille, R., and Thorpe, C. (1994) Electron-transferring flavoprotein from pig and the methylotrophic bacterium W3A1 contains AMP as well as FAD. Biochem. Mol. Biol. Int. 32, 195-199
    • (1994) Biochem. Mol. Biol. Int. , vol.32 , pp. 195-199
    • Duplessis, E.R.1    Rohlfs, R.J.2    Hille, R.3    Thorpe, C.4
  • 8
    • 0019742255 scopus 로고
    • Purification and properties of rat liver acyl-CoA dehydrogenases and electron transfer flavoprotein
    • Furuta, S., Miyazawa, S., and Hashimoto, T. (1981) Purification and properties of rat liver acyl-CoA dehydrogenases and electron transfer flavoprotein. J. Biochem. 90, 1739-1750
    • (1981) J. Biochem. , vol.90 , pp. 1739-1750
    • Furuta, S.1    Miyazawa, S.2    Hashimoto, T.3
  • 9
    • 0020488544 scopus 로고
    • Purification and properties of electron-transferring flavoprotein from pig kidney
    • Gorelick, R.J., Mizzer, J.P., and Thorpe, C. (1982) Purification and properties of electron-transferring flavoprotein from pig kidney. Biochemistry 21, 6936-6942
    • (1982) Biochemistry , vol.21 , pp. 6936-6942
    • Gorelick, R.J.1    Mizzer, J.P.2    Thorpe, C.3
  • 10
    • 0021099167 scopus 로고
    • Subunit structure of electron transfer flavoprotein
    • McKean, M.C., Beckmann, J.D., and Frerman F.E. (1983) Subunit structure of electron transfer flavoprotein. J. Biol. Chem. 258, 1866-1870
    • (1983) J. Biol. Chem. , vol.258 , pp. 1866-1870
    • McKean, M.C.1    Beckmann, J.D.2    Frerman, F.E.3
  • 11
    • 0028037613 scopus 로고
    • Preparation of separated α and β subunits of electron-transferring flavoprotein in unfolded forms and their restoration to the native holoprotein form
    • Sato, K., Nishina, Y., and Shiga, K. (1994) Preparation of separated α and β subunits of electron-transferring flavoprotein in unfolded forms and their restoration to the native holoprotein form. J. Biochem. 116, 147-155
    • (1994) J. Biochem. , vol.116 , pp. 147-155
    • Sato, K.1    Nishina, Y.2    Shiga, K.3
  • 12
    • 0028067411 scopus 로고
    • Crystallization and preliminary crystallographic investigation of electron-transfer flavoprotein from the bacterium Methylophilus W3A1
    • White, S.A., Mathews, F.S., Rohlfs, R.J., and Hille, R. (1994) Crystallization and preliminary crystallographic investigation of electron-transfer flavoprotein from the bacterium Methylophilus W3A1. J. Mol. Biol. 240, 265-266
    • (1994) J. Mol. Biol. , vol.240 , pp. 265-266
    • White, S.A.1    Mathews, F.S.2    Rohlfs, R.J.3    Hille, R.4
  • 13
    • 0029113246 scopus 로고
    • Crystallization and preliminary X-ray analysis of electron transfer flavoproteins from human and Paracoccus denitrificans
    • Roberts, D.L., Herrick, K.R., Frerman, F.E., and Kim, J.-J.P. (1995) Crystallization and preliminary X-ray analysis of electron transfer flavoproteins from human and Paracoccus denitrificans. Protein Sci. 4, 1654-1657
    • (1995) Protein Sci. , vol.4 , pp. 1654-1657
    • Roberts, D.L.1    Herrick, K.R.2    Frerman, F.E.3    Kim, J.-J.P.4
  • 14
    • 0029680251 scopus 로고    scopus 로고
    • In vitro refolding and unfolding of subunits of electron-transferring flavoprotein: Characterization of the folding intermediates and the effects of FAD and AMP on the folding reaction
    • Sato, K., Nishina, Y., and Shiga, K. (1996) In vitro refolding and unfolding of subunits of electron-transferring flavoprotein: Characterization of the folding intermediates and the effects of FAD and AMP on the folding reaction. J. Biochem. 120, 276-285
    • (1996) J. Biochem. , vol.120 , pp. 276-285
    • Sato, K.1    Nishina, Y.2    Shiga, K.3
  • 15
    • 0025761937 scopus 로고
    • The existence of two different forms of apo-electron-transferring flavoprotein
    • Sato, K., Nishina, Y., Shiga, K., Tojo, H., and Tada, M. (1991) The existence of two different forms of apo-electron-transferring flavoprotein. J. Biochem. 109, 734-740
    • (1991) J. Biochem. , vol.109 , pp. 734-740
    • Sato, K.1    Nishina, Y.2    Shiga, K.3    Tojo, H.4    Tada, M.5
  • 17
    • 0000121194 scopus 로고
    • Ultraviolet absorption spectra of adenosine-5′-triphosphate and related 5′-ribonucleotides
    • Bock, R.M., Ling, N.-S., Morell, S.A., and Lipton, S.H. (1956) Ultraviolet absorption spectra of adenosine-5′-triphosphate and related 5′-ribonucleotides. Arch. Biochem. Biophys. 62, 253-264
    • (1956) Arch. Biochem. Biophys. , vol.62 , pp. 253-264
    • Bock, R.M.1    Ling, N.-S.2    Morell, S.A.3    Lipton, S.H.4
  • 18
    • 0024321837 scopus 로고
    • Membrane protein molecular weight determined by low-angel laser light-scattering method coupled with high-performance gel chromatog- Raphy
    • Hayashi, Y., Matsui, H., and Takagi, T. (1989) Membrane protein molecular weight determined by low-angel laser light-scattering method coupled with high-performance gel chromatog- raphy. Methods Enzymol. 172, 514-528
    • (1989) Methods Enzymol. , vol.172 , pp. 514-528
    • Hayashi, Y.1    Matsui, H.2    Takagi, T.3
  • 19
    • 0025299374 scopus 로고
    • Application of low-angle laser light scattering detection in the field of biochemistry
    • Takagi, T. (1990) Application of low-angle laser light scattering detection in the field of biochemistry. J. Chromatogr. 506, 409-416
    • (1990) J. Chromatogr. , vol.506 , pp. 409-416
    • Takagi, T.1
  • 20
    • 0026589431 scopus 로고
    • Anion-induced conformational change of apo-electron-transferring flavoprotein
    • Sato, K., Nishina, Y., and Shiga, K. (1992) Anion-induced conformational change of apo-electron-transferring flavoprotein. J. Biochem. 111, 359-365
    • (1992) J. Biochem. , vol.111 , pp. 359-365
    • Sato, K.1    Nishina, Y.2    Shiga, K.3
  • 21
    • 0027733616 scopus 로고
    • Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule
    • Uversky, V.N. (1993) Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule. Biochemistry 32, 13288-13298
    • (1993) Biochemistry , vol.32 , pp. 13288-13298
    • Uversky, V.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.