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Volumn 222, Issue 8-9, 2008, Pages 1333-1347

Hydrogen tunneling in glucose oxidation by the archaeon Thermoplasma acidophilum

Author keywords

Glucose oxidation; Hydrogen tunneling; Thermoplasma acidophilum

Indexed keywords

GLUCOSE; HYDROGEN; MICROORGANISMS; MOLECULAR BIOLOGY; TEMPERATURE DISTRIBUTION;

EID: 57349195545     PISSN: 09429352     EISSN: None     Source Type: Journal    
DOI: 10.1524/zpch.2008.5391     Document Type: Article
Times cited : (8)

References (25)
  • 2
    • 33748367252 scopus 로고    scopus 로고
    • for the description of a model closely related to that discussed in the present paper. See also
    • See also H.-H. Limbach, J. Miguel Lopez, A. Kohen, Philos Trans. R. Soc. Lond. B Biol. Sci. 361 (2006) 1399-1415 for the description of a model closely related to that discussed in the present paper.
    • (2006) Philos Trans. R. Soc. Lond. B Biol. Sci , vol.361 , pp. 1399-1415
    • Limbach, H.-H.1    Miguel Lopez, J.2    Kohen, A.3
  • 3
    • 84891303633 scopus 로고    scopus 로고
    • J. T. Hynes, J. P. Klinman, H.-H. Limbach, R. L. Schowen Eds, Wiley-VCH, Weinheim
    • Hydrogen-Transfer Reactions. J. T. Hynes, J. P. Klinman, H.-H. Limbach, R. L. Schowen (Eds.), Wiley-VCH, Weinheim (2007).
    • (2007) Hydrogen-Transfer Reactions
  • 5
    • 57349125351 scopus 로고    scopus 로고
    • The Strengths and weaknesses of model reactions for the assessment of tunneling in enzymic reactions. A chapter in Ref. 8
    • In press
    • R. L. Schowen, The Strengths and weaknesses of model reactions for the assessment of tunneling in enzymic reactions. A chapter in Ref. 8. In press.
    • Schowen, R.L.1
  • 8
    • 37149004947 scopus 로고    scopus 로고
    • and (c) B. Hong, F. Maley, A. Kohen, Biochemistry 46 (2007) 14188-14197 for further examples of this phenomenon,
    • and (c) B. Hong, F. Maley, A. Kohen, Biochemistry 46 (2007) 14188-14197 for further examples of this phenomenon,
  • 9
    • 3042709505 scopus 로고    scopus 로고
    • and (d) Z.-X. Liang, T. Lee, K. A. Resing, N. G. Ahn, J. P. Klinman, Proc. Natl. Acad. Sci. USA 101 (2004) 9556-9561 for structural analysis.
    • and (d) Z.-X. Liang, T. Lee, K. A. Resing, N. G. Ahn, J. P. Klinman, Proc. Natl. Acad. Sci. USA 101 (2004) 9556-9561 for structural analysis.
  • 10
    • 33748360130 scopus 로고    scopus 로고
    • P. L. Dutton, A. W. Monroe, N. S. Scrutton, M. J. Sutcliffe, Phil. Trans. Royal Soc. B 361 (2006) 1293-1455. Quantum tunneling in enzymes: beyond the transition state theory paradigm.
    • P. L. Dutton, A. W. Monroe, N. S. Scrutton, M. J. Sutcliffe, Phil. Trans. Royal Soc. B 361 (2006) 1293-1455. Quantum tunneling in enzymes: beyond the transition state theory paradigm.
  • 11
    • 33748593631 scopus 로고    scopus 로고
    • V. Schramm (Ed.), Chem. Rev. 106 (8) (2006) 3029-3496. Principles of enzymatic catalysis.
    • V. Schramm (Ed.), Chem. Rev. 106 (8) (2006) 3029-3496. Principles of enzymatic catalysis.
  • 12
    • 79952746514 scopus 로고    scopus 로고
    • R. Allemann, N. S. Scrutton Eds, Royal Society of Chemistry, London, in press
    • Quantum Tunneling in Enzyme-Catalyzed Reactions. R. Allemann, N. S. Scrutton (Eds.), Royal Society of Chemistry, London, in press.
    • Quantum Tunneling in Enzyme-Catalyzed Reactions
  • 15
    • 0029768821 scopus 로고    scopus 로고
    • M. W. Gray, Nature 383 (1996) 299-300.
    • (1996) Nature , vol.383 , pp. 299-300
    • Gray, M.W.1
  • 16
    • 0032562283 scopus 로고    scopus 로고
    • E. DeLong, Science 280 (1998) 542-543.
    • (1998) Science , vol.280 , pp. 542-543
    • DeLong, E.1
  • 21
    • 0037110531 scopus 로고    scopus 로고
    • J. R. Beasley, D. F. Doyle, L. Chen, B. R. Fine, G. J. Pielak, Proteins Struc. Func. Genet. 49 (2002) 398-402.
    • J. R. Beasley, D. F. Doyle, L. Chen, B. R. Fine, G. J. Pielak, Proteins Struc. Func. Genet. 49 (2002) 398-402.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.