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Volumn 3, Issue 6, 1996, Pages 539-546

The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN;

EID: 0029949340     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0696-539     Document Type: Article
Times cited : (139)

References (21)
  • 1
    • 0028673449 scopus 로고
    • Characterization of 3 proteins containing multiple iron sites - Rubrerythrin, desulforedoxin, and a protein containing a six-iron cluster
    • Moura, I., Tavares, P. & Ravi, N. Characterization of 3 proteins containing multiple iron sites - Rubrerythrin, desulforedoxin, and a protein containing a six-iron cluster. Meth. Enz. 243, 216-240 (1994).
    • (1994) Meth. Enz. , vol.243 , pp. 216-240
    • Moura, I.1    Tavares, P.2    Ravi, N.3
  • 3
    • 0027337927 scopus 로고
    • 57Fe-reconstituted rubrerythrin, a non-heme iron protein with structural analogies to ribonucleotide reductase
    • 57Fe-reconstituted rubrerythrin, a non-heme iron protein with structural analogies to ribonucleotide reductase. Biochemistry 32, 8487-8491 (1993).
    • (1993) Biochemistry , vol.32 , pp. 8487-8491
    • Ravi, N.1    Prickril, B.C.2    Kurtz Jr., D.M.3    Huynh, B.H.4
  • 4
    • 0027511224 scopus 로고
    • Nigerythrin and rubrerythrin from Desulfovibrio vulgaris each contain 2 mononuclear iron centers and 2 dinuclear iron clusters
    • Pierik, A.J., Wolbert, R.B.G., Portier, G.L., Verhagen, M.F.J.M. & Hagen, W.R. Nigerythrin and rubrerythrin from Desulfovibrio vulgaris each contain 2 mononuclear iron centers and 2 dinuclear iron clusters. European Journal of Biochemistry 212, 237-245 (1993).
    • (1993) European Journal of Biochemistry , vol.212 , pp. 237-245
    • Pierik, A.J.1    Wolbert, R.B.G.2    Portier, G.L.3    Verhagen, M.F.J.M.4    Hagen, W.R.5
  • 5
    • 0028942712 scopus 로고
    • Recombinant Desulfovibrio vulgaris rubrerythrin. Isolation and characterization of the diiron domain
    • Gupta, N. et al. Recombinant Desulfovibrio vulgaris rubrerythrin. Isolation and characterization of the diiron domain. Biochemistry 34, 3310-3318 (1995).
    • (1995) Biochemistry , vol.34 , pp. 3310-3318
    • Gupta, N.1
  • 6
    • 0026347046 scopus 로고
    • Cloning and sequencing of the gene for Rubrerythrin from Desulfovibrio vulgaris (Hildenborough)
    • Prickril, B.C., Kurtz, D.M., Jr., LeGall, J. & Voordouw, G. Cloning and sequencing of the gene for Rubrerythrin from Desulfovibrio vulgaris (Hildenborough). Biochemistry 30, 11118-11123 (1991).
    • (1991) Biochemistry , vol.30 , pp. 11118-11123
    • Prickril, B.C.1    Kurtz Jr., D.M.2    LeGall, J.3    Voordouw, G.4
  • 7
    • 0026318136 scopus 로고
    • Intrapeptide sequence homology in rubrerythrin from Desulfovibrio vulgaris: Identification of potential ligands to the diiron site
    • Kurtz, D.M., Jr. & Prickril, B.C. Intrapeptide sequence homology in rubrerythrin from Desulfovibrio vulgaris: Identification of potential ligands to the diiron site. Biochemical and Biophysical Research Communications 181, 337-341 (1991).
    • (1991) Biochemical and Biophysical Research Communications , vol.181 , pp. 337-341
    • Kurtz Jr., D.M.1    Prickril, B.C.2
  • 9
    • 0027913094 scopus 로고
    • Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane
    • Rosenzweig, A.C., Frederick, C.A., Lippard, S.J. & Nordlund, P. Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane. Nature 366, 537-543 (1993).
    • (1993) Nature , vol.366 , pp. 537-543
    • Rosenzweig, A.C.1    Frederick, C.A.2    Lippard, S.J.3    Nordlund, P.4
  • 11
    • 0025293287 scopus 로고
    • Three dimensional structure of the free radical protein of ribonucleotide reductase
    • Nordlund, P., Sjöberg, B.-M. & Eklund, H. Three dimensional structure of the free radical protein of ribonucleotide reductase. Nature 345, 593-598 (1990).
    • (1990) Nature , vol.345 , pp. 593-598
    • Nordlund, P.1    Sjöberg, B.-M.2    Eklund, H.3
  • 12
    • 0027283896 scopus 로고
    • Structure and function of the Escherichia coli ribonucleotide reductase protein R2
    • Nordlund, P. & Eklund, H. Structure and function of the Escherichia coli ribonucleotide reductase protein R2. J. Mol. Biol. 231, 123-164 (1993).
    • (1993) J. Mol. Biol. , vol.231 , pp. 123-164
    • Nordlund, P.1    Eklund, H.2
  • 13
    • 0001614967 scopus 로고
    • The dissimilatory sulphate-reducing and sulfur-reducing bacteria
    • eds. A. Balows, H.G. Dworkin, W. Harder, & K.H. Schleifer Springer-Verlag, New York
    • Widell, L.C. & Hansen, T.A. The dissimilatory sulphate-reducing and sulfur-reducing bacteria, in The Prokaryotes (eds. A. Balows, H.G. Dworkin, W. Harder, & K.H. Schleifer) 583-624 (Springer-Verlag, New York, 1992).
    • (1992) The Prokaryotes , pp. 583-624
    • Widell, L.C.1    Hansen, T.A.2
  • 14
    • 0024996440 scopus 로고
    • Purification and characterization of two proteins with inorganic pyrophosphatase activity from Desulfovibrio vulgaris: Rubrerythrin and a new, highly active, enzyme
    • Liu, M.Y. & LeGall, J. Purification and characterization of two proteins with inorganic pyrophosphatase activity from Desulfovibrio vulgaris: Rubrerythrin and a new, highly active, enzyme, Biochem. Biophys. Res. Commun. 171, 316-318 (1990).
    • (1990) Biochem. Biophys. Res. Commun. , vol.171 , pp. 316-318
    • Liu, M.Y.1    LeGall, J.2
  • 15
    • 0009411657 scopus 로고
    • Reactions of non-heme iron (II)centers with dioxygen in biology and chemistry
    • Feig, A.L. & Lippard, S.J. Reactions of non-heme iron (II)centers with dioxygen in biology and chemistry. Chemical Reviews 94, 759-805 (1994).
    • (1994) Chemical Reviews , vol.94 , pp. 759-805
    • Feig, A.L.1    Lippard, S.J.2
  • 16
    • 0004120302 scopus 로고
    • Iron: Proteins with dinuclear active sites
    • ed. King, R.B. Wiley, Chichester, UK
    • Kurtz, D.M., Jr. Iron: Proteins with dinuclear active sites in Encyclopedia of Inorganic Chemistry (ed. King, R.B.) 1847-1859 (Wiley, Chichester, UK, 1994).
    • (1994) Encyclopedia of Inorganic Chemistry , pp. 1847-1859
    • Kurtz Jr., D.M.1
  • 17
    • 0000043761 scopus 로고
    • Dioxygen and hemerythrin
    • Stenkamp, R.E. Dioxygen and hemerythrin. Chemical Reviews 94, 715-726 (1994).
    • (1994) Chemical Reviews , vol.94 , pp. 715-726
    • Stenkamp, R.E.1
  • 18
    • 0028170957 scopus 로고
    • Resonance Raman evidence for anFe-O-Fe center in stearoyl-ACP destaurase. Primary sequence identity with other diiron-oxo proteins
    • Fox, B.G., Shanklin, J., Ai, J., Loehr, T.M. & Sanders-Loehr, J. Resonance Raman evidence for anFe-O-Fe center in stearoyl-ACP destaurase. Primary sequence identity with other diiron-oxo proteins. Biochemistry 33, 12776-12786 (1994).
    • (1994) Biochemistry , vol.33 , pp. 12776-12786
    • Fox, B.G.1    Shanklin, J.2    Ai, J.3    Loehr, T.M.4    Sanders-Loehr, J.5
  • 19
    • 0001346095 scopus 로고
    • Ferritin
    • ed.&(eds. Loehr, T.M.) VCH Publishers, New York
    • Harrison, P. & Lilley, T.H. Ferritin in Iron Carriers and Iron Proteins (ed.&(eds. Loehr, T.M.) 123-237 (VCH Publishers, New York, 1989).
    • (1989) Iron Carriers and Iron Proteins , pp. 123-237
    • Harrison, P.1    Lilley, T.H.2
  • 20
    • 0028067272 scopus 로고
    • Direct observation of the iron binding sites in a ferritin
    • Hempstead, P.D. et al. Direct observation of the iron binding sites in a ferritin. FEBS Letters 350, 258-262 (1994).
    • (1994) FEBS Letters , vol.350 , pp. 258-262
    • Hempstead, P.D.1
  • 21
    • 0028467772 scopus 로고
    • Structure of a unique two-fold symmetric haem-binding site
    • Frolow, F., Kalb(Gilboa), J. & Yariv, J. Structure of a unique two-fold symmetric haem-binding site. Nature Struct. Biology 1, 453-460 (1994).
    • (1994) Nature Struct. Biology , vol.1 , pp. 453-460
    • Frolow, F.1    Kalb, J.2    Yariv, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.