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Volumn 1784, Issue 11, 2008, Pages 1596-1600

On the relative contribution of ionic interactions over iron-sulfur clusters to ferredoxin stability

Author keywords

Biophysics; Iron sulfur cluster; Metal; pH stability; Protein folding; Thermal stability; Thermophilic protein

Indexed keywords

FERREDOXIN; IRON SULFUR PROTEIN;

EID: 54049123709     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.05.001     Document Type: Article
Times cited : (7)

References (22)
  • 1
    • 0027995384 scopus 로고
    • Classification of acid denaturation of proteins: intermediates and unfolded states
    • Fink A.L., Calciano L.J., Goto Y., Kurotsu T., and Palleros D.R. Classification of acid denaturation of proteins: intermediates and unfolded states. Biochemistry 33 (1994) 12504-12511
    • (1994) Biochemistry , vol.33 , pp. 12504-12511
    • Fink, A.L.1    Calciano, L.J.2    Goto, Y.3    Kurotsu, T.4    Palleros, D.R.5
  • 2
    • 0036005637 scopus 로고    scopus 로고
    • Role of cofactors in protein folding
    • Wittung-Stafshede P. Role of cofactors in protein folding. Acc. Chem. Res. 35 (2002) 201-208
    • (2002) Acc. Chem. Res. , vol.35 , pp. 201-208
    • Wittung-Stafshede, P.1
  • 3
    • 0031414716 scopus 로고    scopus 로고
    • Energetics of heme binding to native and denatured states of cytochrome b562
    • Robinson C.R., Liu Y., Thomson J.A., Sturtevant J.M., and Sligar S.G. Energetics of heme binding to native and denatured states of cytochrome b562. Biochemistry 36 (1997) 16141-16146
    • (1997) Biochemistry , vol.36 , pp. 16141-16146
    • Robinson, C.R.1    Liu, Y.2    Thomson, J.A.3    Sturtevant, J.M.4    Sligar, S.G.5
  • 4
    • 33645506272 scopus 로고    scopus 로고
    • Cofactor effects on the protein folding reaction: acceleration of alpha-lactalbumin refolding by metal ions
    • Bushmarina N.A., Blanchet C.E., Vernier G., and Forge V. Cofactor effects on the protein folding reaction: acceleration of alpha-lactalbumin refolding by metal ions. Protein Sci. 15 (2006) 659-671
    • (2006) Protein Sci. , vol.15 , pp. 659-671
    • Bushmarina, N.A.1    Blanchet, C.E.2    Vernier, G.3    Forge, V.4
  • 7
    • 39649092718 scopus 로고    scopus 로고
    • Crystallographic analysis of the intact metal centres [3Fe-4 S](1+/0) and [4Fe-4S](2+/1+) in a Zn(2+)-containing ferredoxin
    • Frazao C., Aragao D., Coelho R., Leal S.S., Gomes C.M., Teixeira M., and Carrondo M.A. Crystallographic analysis of the intact metal centres [3Fe-4 S](1+/0) and [4Fe-4S](2+/1+) in a Zn(2+)-containing ferredoxin. FEBS Lett. 582 (2008) 763-767
    • (2008) FEBS Lett. , vol.582 , pp. 763-767
    • Frazao, C.1    Aragao, D.2    Coelho, R.3    Leal, S.S.4    Gomes, C.M.5    Teixeira, M.6    Carrondo, M.A.7
  • 8
    • 0034926051 scopus 로고    scopus 로고
    • High stability of a ferredoxin from the hyperthermophilic archaeon A. ambivalens: involvement of electrostatic interactions and cofactors
    • Moczygemba C., Guidry J., Jones K.L., Gomes C.M., Teixeira M., and Wittung-Stafshede P. High stability of a ferredoxin from the hyperthermophilic archaeon A. ambivalens: involvement of electrostatic interactions and cofactors. Protein Sci. 10 (2001) 1539-1548
    • (2001) Protein Sci. , vol.10 , pp. 1539-1548
    • Moczygemba, C.1    Guidry, J.2    Jones, K.L.3    Gomes, C.M.4    Teixeira, M.5    Wittung-Stafshede, P.6
  • 9
    • 34548694529 scopus 로고    scopus 로고
    • A spectroscopic study of the temperature induced modifications on ferredoxin folding and iron-sulfur moieties
    • Todorovic S., Leal S.S., Salgueiro C.A., Zebger I., Hildebrandt P., Murgida D.H., and Gomes C.M. A spectroscopic study of the temperature induced modifications on ferredoxin folding and iron-sulfur moieties. Biochemistry 46 (2007) 10733-10738
    • (2007) Biochemistry , vol.46 , pp. 10733-10738
    • Todorovic, S.1    Leal, S.S.2    Salgueiro, C.A.3    Zebger, I.4    Hildebrandt, P.5    Murgida, D.H.6    Gomes, C.M.7
  • 11
    • 0031551572 scopus 로고    scopus 로고
    • Ferredoxin from the hyperthermophile Thermotoga maritima is stable beyond the boiling point of water
    • Pfeil W., Gesierich U., Kleemann G.R., and Sterner R. Ferredoxin from the hyperthermophile Thermotoga maritima is stable beyond the boiling point of water. J. Mol. Biol. 272 (1997) 591-596
    • (1997) J. Mol. Biol. , vol.272 , pp. 591-596
    • Pfeil, W.1    Gesierich, U.2    Kleemann, G.R.3    Sterner, R.4
  • 12
    • 0346500473 scopus 로고    scopus 로고
    • Folding and association of an extremely stable dimeric protein from Sulfolobus islandicus
    • Zeeb M., Lipps G., Lilie H., and Balbach J. Folding and association of an extremely stable dimeric protein from Sulfolobus islandicus. J. Mol. Biol. 336 (2004) 227-240
    • (2004) J. Mol. Biol. , vol.336 , pp. 227-240
    • Zeeb, M.1    Lipps, G.2    Lilie, H.3    Balbach, J.4
  • 14
    • 0034651201 scopus 로고    scopus 로고
    • Stability and folding of the ferredoxin from the hyperthermophilic archaeon Acidianus ambivalens
    • Wittung-Stafshede P., Gomes C.M., and Teixeira M. Stability and folding of the ferredoxin from the hyperthermophilic archaeon Acidianus ambivalens. J. Inorg. Biochem. 78 (2000) 35-41
    • (2000) J. Inorg. Biochem. , vol.78 , pp. 35-41
    • Wittung-Stafshede, P.1    Gomes, C.M.2    Teixeira, M.3
  • 16
    • 0036902235 scopus 로고    scopus 로고
    • Close-range electrostatic interactions in proteins
    • Kumar S., and Nussinov R. Close-range electrostatic interactions in proteins. Chembiochem 3 (2002) 604-617
    • (2002) Chembiochem , vol.3 , pp. 604-617
    • Kumar, S.1    Nussinov, R.2
  • 17
    • 0037432563 scopus 로고    scopus 로고
    • Contribution of surface salt bridges to protein stability: guidelines for protein engineering
    • Makhatadze G.I., Loladze V.V., Ermolenko D.N., Chen X., and Thomas S.T. Contribution of surface salt bridges to protein stability: guidelines for protein engineering. J. Mol. Biol. 327 (2003) 1135-1148
    • (2003) J. Mol. Biol. , vol.327 , pp. 1135-1148
    • Makhatadze, G.I.1    Loladze, V.V.2    Ermolenko, D.N.3    Chen, X.4    Thomas, S.T.5
  • 18
    • 33748694511 scopus 로고    scopus 로고
    • Natural domain design: enhanced thermal stability of a zinc-lacking ferredoxin isoform shows that a hydrophobic core efficiently replaces the structural metal site
    • Rocha R., Leal S.S., Teixeira V.H., Regalla M., Huber H., Baptista A.M., Soares C.M., and Gomes C.M. Natural domain design: enhanced thermal stability of a zinc-lacking ferredoxin isoform shows that a hydrophobic core efficiently replaces the structural metal site. Biochemistry 45 (2006) 10376-10384
    • (2006) Biochemistry , vol.45 , pp. 10376-10384
    • Rocha, R.1    Leal, S.S.2    Teixeira, V.H.3    Regalla, M.4    Huber, H.5    Baptista, A.M.6    Soares, C.M.7    Gomes, C.M.8
  • 19
    • 34447549197 scopus 로고    scopus 로고
    • Studies of the molten globule state of ferredoxin: structural characterization and implications on protein folding and iron-sulfur center assembly
    • Leal S.S., and Gomes C.M. Studies of the molten globule state of ferredoxin: structural characterization and implications on protein folding and iron-sulfur center assembly. Proteins 68 (2007) 606-616
    • (2007) Proteins , vol.68 , pp. 606-616
    • Leal, S.S.1    Gomes, C.M.2
  • 20
    • 0029090926 scopus 로고
    • Response of rubredoxin from Pyrococcus furiosus to environmental changes: implications for the origin of hyperthermostability
    • Cavagnero S., Zhou Z.H., Adams M.W., and Chan S.I. Response of rubredoxin from Pyrococcus furiosus to environmental changes: implications for the origin of hyperthermostability. Biochemistry 34 (1995) 9865-9873
    • (1995) Biochemistry , vol.34 , pp. 9865-9873
    • Cavagnero, S.1    Zhou, Z.H.2    Adams, M.W.3    Chan, S.I.4
  • 21
    • 0035808359 scopus 로고    scopus 로고
    • Low pH-induced conformational changes in vesicular stomatitis virus glycoprotein involve dramatic structure reorganization
    • Carneiro F.A., Ferradosa A.S., and Da Poian A.T. Low pH-induced conformational changes in vesicular stomatitis virus glycoprotein involve dramatic structure reorganization. J. Biol. Chem. 276 (2001) 62-67
    • (2001) J. Biol. Chem. , vol.276 , pp. 62-67
    • Carneiro, F.A.1    Ferradosa, A.S.2    Da Poian, A.T.3
  • 22
    • 54049115632 scopus 로고    scopus 로고
    • Encyclopedia of Life Sciences
    • Fink A.L. Molten Globule (2001), Encyclopedia of Life Sciences
    • (2001) Molten Globule
    • Fink, A.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.