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Volumn 99, Issue 7, 2010, Pages

On the question of hydronium binding to ATP-Synthase membrane rotors

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EID: 77958507494     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.07.046     Document Type: Article
Times cited : (20)

References (19)
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    • Pogoryelov, D.1    Yildiz, O.2    Meier, T.3
  • 8
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    • 14 rotor ring of the proton translocating chloroplast ATP synthase. J. Biol. Chem. 284:18228-18235.
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  • 10
    • 0023825249 scopus 로고
    • Bioenergetic coupling to protonmotive force: Should we be considering hydronium ion coordination and not group proton- ation?
    • Boyer, P. D. 1988. Bioenergetic coupling to protonmotive force: should we be considering hydronium ion coordination and not group proton- ation? Trends Biochem. Sci. 13:5-7.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 5-7
    • Boyer, P.D.1
  • 11
    • 0000406218 scopus 로고
    • + cation: Molecular structure of an oxonium macrocyclic polyether complex
    • + cation: molecular structure of an oxonium macrocyclic polyether complex. J. Am. Chem. Soc. 104:4540-4543.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4540-4543
    • Behr, J.P.1    Dumas, P.2    Moras, D.3
  • 12
    • 35448959682 scopus 로고    scopus 로고
    • Two distinct proton binding sites in the ATP synthase family
    • von Ballmoos, C., and P. Dimroth. 2007. Two distinct proton binding sites in the ATP synthase family. Biochemistry. 46:11800-11809.
    • (2007) Biochemistry , vol.46 , pp. 11800-11809
    • Von Ballmoos, C.1    Dimroth, P.2
  • 13
    • 67649482445 scopus 로고    scopus 로고
    • A more robust version of the Arginine 210-switched mutant in subunit a of the Escherichia coli ATP synthase
    • Bae, L., and S. B. Vik. 2009. A more robust version of the Arginine 210-switched mutant in subunit a of the Escherichia coli ATP synthase. Biochim. Biophys. Acta. 1787:1129-1134.
    • (2009) Biochim. Biophys. Acta. , vol.1787 , pp. 1129-1134
    • Bae, L.1    Vik, S.B.2
  • 15
    • 0742305361 scopus 로고    scopus 로고
    • Mechanism of proton transport by plant plasma membrane proton ATPases
    • Buch-Pedersen, M. J., and M. G. Palmgren. 2003. Mechanism of proton transport by plant plasma membrane proton ATPases. J. Plant Res. 116:507-515.
    • (2003) J. Plant Res. , vol.116 , pp. 507-515
    • Buch-Pedersen, M.J.1    Palmgren, M.G.2
  • 17
    • 34147112824 scopus 로고    scopus 로고
    • Structure and energetics of the hydronium hydration shells
    • Markovitch, O., and N. Agmon. 2007. Structure and energetics of the hydronium hydration shells. J. Phys. Chem. A. 111:2253-2256.
    • (2007) J. Phys. Chem. A. , vol.111 , pp. 2253-2256
    • Markovitch, O.1    Agmon, N.2
  • 19
    • 34547732425 scopus 로고    scopus 로고
    • The oligomeric state of c rings from cyanobacterial F-ATP synthases varies from 13 to 15
    • Pogoryelov, D., C. Reichen, T. Meier. 2007. The oligomeric state of c rings from cyanobacterial F-ATP synthases varies from 13 to 15. J. Bacteriol. 189:5895-5902.
    • (2007) J. Bacteriol. , vol.189 , pp. 5895-5902
    • Pogoryelov, D.1    Reichen, C.2    Meier, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.