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Volumn 119, Issue 31, 1997, Pages 7181-7189

Infrared-spectroelectrochemical characterization of the [NiFe] hydrogenase of Desulfovibrio gigas

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGENASE;

EID: 0030805822     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja963802w     Document Type: Article
Times cited : (260)

References (41)
  • 23
    • 1842331694 scopus 로고    scopus 로고
    • note
    • Although all three bands of each redox state titrate simultaneously, only the one with lowest frequency is taken into acount as it is much more intense than the other two and because some states have in common the frequency of one of the less intense bands.
  • 24
    • 1842297138 scopus 로고    scopus 로고
    • note
    • 1914 could not be obtained because the enzyme was not stable at pH 10.5.
  • 31
    • 0003481596 scopus 로고
    • W. H. Freeman and Company: San Francisco
    • Fersht, A. In Enzyme Structure and Mechanism; W. H. Freeman and Company: San Francisco, 1977; p 2.
    • (1977) Enzyme Structure and Mechanism , pp. 2
    • Fersht, A.1
  • 34
    • 1842298313 scopus 로고    scopus 로고
    • note
    • Although the IR-spectroelectrochemical cell is not completely gas tight, the oxygen that diffuses into the cell is quickly reduced by the redox mediators present in the sample, therefore anaerobic conditions are maintained.
  • 36
    • 1842287558 scopus 로고    scopus 로고
    • note
    • m at pH = 8.0 shown in this scheme have been calculated from those of Table 2 by taking into account their dependence of the pH, as determined in this work The states for which Ni is EPR-detectable are marked with an asterisk.
  • 37
    • 1842301283 scopus 로고    scopus 로고
    • note
    • The electron balance of SU conversion to SI form has not yet been quantified.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.