메뉴 건너뛰기




Volumn 48, Issue 1, 1999, Pages 87-93

Studies on the heme and H2-uptake reaction from Azotobacter vinelandii bacterial ferritin

Author keywords

Activity of nitrogen fixation; Azotobacter vinelandii; Bacterial ferritin; Electrode activity; Electron tunnel heme Co2+; Iron release; Role of H2 uptake

Indexed keywords

BACTERIA; ELECTROCHEMICAL ELECTRODES; HYDROGEN; MOLECULAR STRUCTURE; NITROGEN FIXATION; PLATINUM; REDUCTION; SYNTHESIS (CHEMICAL);

EID: 0032587352     PISSN: 03024598     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0302-4598(98)00215-3     Document Type: Article
Times cited : (8)

References (25)
  • 1
    • 0023067301 scopus 로고
    • Ferritin: Structure, gene, regulation, and cellular function in animals, plant,and microorganisms
    • Theil E.C. Ferritin: structure, gene, regulation, and cellular function in animals, plant,and microorganisms. Annu. Rev. Biochem. 56:1987;289-315.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 289-315
    • Theil, E.C.1
  • 3
    • 0026235509 scopus 로고
    • The visualization of apoferritin in the secretory pathway of vertebrate liver cells
    • Renaud D.L., Nichol H., Locke M. The visualization of apoferritin in the secretory pathway of vertebrate liver cells. J. Subnicrosc. Cytol. Pathol. 23:1993;501-507.
    • (1993) J. Subnicrosc. Cytol. Pathol. , vol.23 , pp. 501-507
    • Renaud, D.L.1    Nichol, H.2    Locke, M.3
  • 4
    • 6844266253 scopus 로고    scopus 로고
    • H2-uptake activity, spectra, reduction potentials, and kinetics of iron release on the surface of iron core from Azotobacter vinelandii bacterial ferritin
    • Huang H.Q., Xu L.S., Zhang F.Z., Qiu X.H., Lin Q.M., Huang J.W., Zao H., Huang N.C., Zeng R.Y., Zeng D. H2-uptake activity, spectra, reduction potentials, and kinetics of iron release on the surface of iron core from Azotobacter vinelandii bacterial ferritin. J. Protein Chem. 17:1998;45-52.
    • (1998) J. Protein Chem. , vol.17 , pp. 45-52
    • Huang, H.Q.1    Xu, L.S.2    Zhang, F.Z.3    Qiu, X.H.4    Lin, Q.M.5    Huang, J.W.6    Zao, H.7    Huang, N.C.8    Zeng, R.Y.9    Zeng, D.10
  • 5
  • 6
    • 0006538337 scopus 로고    scopus 로고
    • Comparison of physio-chemical properties of ferritin between pig and horse spleen
    • Huang H.Q., Zhang F.Z., Xu L.S. Comparison of physio-chemical properties of ferritin between pig and horse spleen. Acta Zoologica Sinica. 43:1997;170-177.
    • (1997) Acta Zoologica Sinica , vol.43 , pp. 170-177
    • Huang, H.Q.1    Zhang, F.Z.2    Xu, L.S.3
  • 9
    • 0018123699 scopus 로고
    • Mechanism and kinetics of iron release from ferritin by dihydroflavins and dihydroflavin analogues
    • Jones T., Spencer R., Walsh C. Mechanism and kinetics of iron release from ferritin by dihydroflavins and dihydroflavin analogues. Biochemistry. 17:1978;4011-4017.
    • (1978) Biochemistry , vol.17 , pp. 4011-4017
    • Jones, T.1    Spencer, R.2    Walsh, C.3
  • 10
    • 0345250426 scopus 로고    scopus 로고
    • Transfer of the reaction orders and the phases numbers of rate for iron release from horse spleen ferritin
    • (in press)
    • H.Q. Huang, F.Z. Zhang, Q.M. Lin, Q.X Fui, L.S. Xu. Transfer of the reaction orders and the phases numbers of rate for iron release from horse spleen ferritin. Acta Zoologica Sinica (in press).
    • Acta Zoologica Sinica
    • Huang, H.Q.1    Zhang, F.Z.2    Lin, Q.M.3    Fui, Q.X.4    L.S., Xu.5
  • 11
    • 0030021369 scopus 로고    scopus 로고
    • A kinetic studyies of iron release from Azotobacter vinelandii bacterial ferritin
    • Richards T.D., Pitts K.R., Watt G.D. A kinetic studyies of iron release from Azotobacter vinelandii bacterial ferritin. J. Inorg. Biochem. 61:1996;1-13.
    • (1996) J. Inorg. Biochem. , vol.61 , pp. 1-13
    • Richards, T.D.1    Pitts, K.R.2    Watt, G.D.3
  • 13
    • 0031029483 scopus 로고    scopus 로고
    • Dinuclear center of ferritin: Studies of iron binding and oxidation show differences in the two iron sites
    • Treffry A., Zhao Z.G., Quail M.A., Guest J.R., Harrison P.M. Dinuclear center of ferritin: studies of iron binding and oxidation show differences in the two iron sites. Biochemistry. 36:1997;432-441.
    • (1997) Biochemistry , vol.36 , pp. 432-441
    • Treffry, A.1    Zhao, Z.G.2    Quail, M.A.3    Guest, J.R.4    Harrison, P.M.5
  • 14
    • 0027301391 scopus 로고
    • Nucleation of the iron n core occurs at the three-fold channels of horse spleen apoferritin: An EXAFS studies on the native and chemically-modified protein
    • Strange R., Morante S., Stefanini S., Chianocone E., Desideri A. Nucleation of the iron n core occurs at the three-fold channels of horse spleen apoferritin: an EXAFS studies on the native and chemically-modified protein. Biochim. Biophys. Acta. 1164:1993;31-334.
    • (1993) Biochim. Biophys. Acta , vol.1164 , pp. 31-334
    • Strange, R.1    Morante, S.2    Stefanini, S.3    Chianocone, E.4    Desideri, A.5
  • 15
    • 0016173575 scopus 로고
    • The release of iron from horse spleen by reduced flavins
    • Sirivech S., Frieden E., Osaki S. The release of iron from horse spleen by reduced flavins. Biochem. J. 143:1974;311-315.
    • (1974) Biochem. J. , vol.143 , pp. 311-315
    • Sirivech, S.1    Frieden, E.2    Osaki, S.3
  • 16
    • 0009460803 scopus 로고
    • The properties of the surface of iron core from horse spleen ferritin
    • Huang H.Q., Watt R.K., Frankel R.B., Watt G.D. The properties of the surface of iron core from horse spleen ferritin. J. Xiamen Univ. 32:1993;628-633.
    • (1993) J. Xiamen Univ. , vol.32 , pp. 628-633
    • Huang, H.Q.1    Watt, R.K.2    Frankel, R.B.3    Watt, G.D.4
  • 17
    • 0000865399 scopus 로고
    • Redox properties and Mossbauer spectroscopy of azotobacter vinelandii bacterioferritin
    • Watt G.D., Frankel R.B., Papaefthymiou G.C., Spartalian K., Stiefel E.I. Redox properties and Mossbauer spectroscopy of azotobacter vinelandii bacterioferritin. Biochemistry. 25:1986;4330-4336.
    • (1986) Biochemistry , vol.25 , pp. 4330-4336
    • Watt, G.D.1    Frankel, R.B.2    Papaefthymiou, G.C.3    Spartalian, K.4    Stiefel, E.I.5
  • 18
    • 0027363945 scopus 로고
    • Further characteristics of the redox and spectroscopic properties of Azotobacter vinelandii bacterial ferritin
    • Watt G.D., Mcdonald J.W., Chiu C.H., Reddy K.R.N. Further characteristics of the redox and spectroscopic properties of Azotobacter vinelandii bacterial ferritin. J. Inorg. Biochem. 51:1992;745-758.
    • (1992) J. Inorg. Biochem. , vol.51 , pp. 745-758
    • Watt, G.D.1    McDonald, J.W.2    Chiu, C.H.3    Reddy, K.R.N.4
  • 19
    • 0026611229 scopus 로고
    • 2+ and phosphate interactions in bacterial ferritin from Azotobacter vinelandii
    • 2+ and phosphate interactions in bacterial ferritin from Azotobacter vinelandii. Biochemistry. 31:1993;745-758.
    • (1993) Biochemistry , vol.31 , pp. 745-758
    • Watt, G.D.1    Frankel, R.B.2    Jacobs, D.3    Huang, H.Q.4
  • 20
    • 0015698350 scopus 로고
    • A hemoprotein from azotobacter containing non-heme iron: Isolation and crystallization
    • Bulen W.A., leComte R., Lough S. A hemoprotein from azotobacter containing non-heme iron: isolation and crystallization. Biochem. Biophys. Res. Commun. 54:1973;1274-1281.
    • (1973) Biochem. Biophys. Res. Commun. , vol.54 , pp. 1274-1281
    • Bulen, W.A.1    Lecomte, R.2    Lough, S.3
  • 21
    • 0019321298 scopus 로고
    • Large-scale purification of high activity Azotobacter vinelandii nitrogenase
    • Burgess B.K., Jacobs D.B., Stiefel E.I. Large-scale purification of high activity Azotobacter vinelandii nitrogenase. Biochem. Biophys. Acta. 614:1980;196-209.
    • (1980) Biochem. Biophys. Acta , vol.614 , pp. 196-209
    • Burgess, B.K.1    Jacobs, D.B.2    Stiefel, E.I.3
  • 24
    • 0021757851 scopus 로고
    • A nitrogen pressure of 50 atmosphere does prevent evolution of hydrogen by nitrogenase
    • Simpson F.B., Burris R.H. A nitrogen pressure of 50 atmosphere does prevent evolution of hydrogen by nitrogenase. Science. 224:1984;1095-1097.
    • (1984) Science , vol.224 , pp. 1095-1097
    • Simpson, F.B.1    Burris, R.H.2
  • 25
    • 0018333857 scopus 로고
    • Azotobacter cytochrome b557.5 is a bacterioferritin
    • Stiefel E.I., Watt G.D. Azotobacter cytochrome b557.5 is a bacterioferritin. Nature. 279:1979;81-83.
    • (1979) Nature , vol.279 , pp. 81-83
    • Stiefel, E.I.1    Watt, G.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.