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Volumn 127, Issue 50, 2005, Pages 17954-17961

Oxygen- and temperature-dependent kinetic isotope effects in choline oxidase: Correlating reversible hydride transfer with environmentally enhanced tunneling

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDES; CONCENTRATION (PROCESS); ELECTRON TUNNELING; ENZYMES; HYDRIDES; OXIDATION; OXYGEN; QUANTUM THEORY; REACTION KINETICS;

EID: 29344449107     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0560377     Document Type: Article
Times cited : (51)

References (49)
  • 2
    • 0024298964 scopus 로고
    • Kraut, J. Science 1988, 242, 533-40.
    • (1988) Science , vol.242 , pp. 533-540
    • Kraut, J.1
  • 27
    • 29344471680 scopus 로고    scopus 로고
    • unpublished data
    • The three-dimensional structure of choline oxidase is available at a resolution of 1.86 Å by X-ray crystallography (George Lountos, Fan Fan, Giovanni Gadda, and Allen M. Orville; unpublished data).
    • Lountos, G.1    Fan, F.2    Gadda, G.3    Orville, A.M.4
  • 37
    • 29344450017 scopus 로고    scopus 로고
    • note
    • b} could not be used for the determination of deuterium isotope effects under steady-state conditions.
  • 38
    • 29344449761 scopus 로고    scopus 로고
    • note
    • m values for oxygen when choline is used as substrate for choline oxidase range from 0.1 mM at pH 6 to 1.6 mM at pH 10 (Fan Fan and Giovanni Gadda; unpublished results). Consequently, at a concentration of oxygen of 0.25 mM. i.e., at atmospheric oxygen, the enzyme is not saturated with oxygen.
  • 39
    • 0018815070 scopus 로고
    • Purich, D. L., Ed.; Academic Press: New York
    • m) value of ∼10.6 at saturating oxygen concentrations after accounting for an α-secondary effect of 1.24 and two β-secondary effects of 1.05 (for references, see: Cleland, W. W. In Methods in Enzymology; Purich, D. L., Ed.; Academic Press: New York. 1980; Vol. 64, pp 104-25.
    • (1980) Methods in Enzymology , vol.64 , pp. 104-125
    • Cleland, W.W.1
  • 42
    • 29344473808 scopus 로고    scopus 로고
    • note
    • D′) of the preexponential factors. Since the linear fits of the two sets of data in Figure 3 have small standard deviations, the isotope effect on the preexponential factors estimated in this fashion has a small standard deviation.
  • 43
    • 85056434067 scopus 로고    scopus 로고
    • Kohen, A., Limbach, H. H., Eds.; Taylor & Francis. CRC Press: New York, Chapter 37
    • Cleland, W. W. In Isotope Effects in Chemistry and Biology; Kohen, A., Limbach, H. H., Eds.; Taylor & Francis. CRC Press: New York, 2005; Chapter 37, pp 915-30.
    • (2005) Isotope Effects in Chemistry and Biology , pp. 915-930
    • Cleland, W.W.1
  • 46
    • 0018815070 scopus 로고
    • Measurement of isotope effect by the equilibrium perturbation technique
    • Purich, D. L., Ed. Academic Press: New York
    • Cleland, W. W. Measurement of isotope effect by the equilibrium perturbation technique. In Methods in Enzymology; Purich, D. L., Ed. Academic Press: New York, 1980; Vol. 64, pp 104-125.
    • (1980) Methods in Enzymology , vol.64 , pp. 104-125
    • Cleland, W.W.1
  • 47
    • 29344434748 scopus 로고    scopus 로고
    • note
    • 2].


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.