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  • Journal
    Digital Access
    Provider
    Version
    ScienceDirect
    v. 66-, 2005-
    ClinicalKey
    v. 68-, 2007-
    PubMed Central
    v. 74-, 2013-
    ScienceDirect
    v. 52-55, 1992-94.
    Print Access Request
    Location
    Version
    Call Number
    Items
    Stored offsite. Please request print.
    v. 1-55, 1959-94.
    74
  • Article
    Brockman HL, Wood WA.
    J Bacteriol. 1975 Dec;124(3):1454-61.
    D-Lactate dehydrogenase has been purified to near homogeneity from Peptostreptococcus elsdenii. As isolated, the enzyme contains flavine adenine dinucleotide and a tightly bound metal cofactor. Inactivation by ortho-phenanthroline occurs in two steps and is partially blocked by D-lactate. Reactivation by divalent metal ions occurs, with divalent zinc being the most effective. When ferricyanide is used as the electron acceptor, D-lactate has an apparent K0.5 of 3.3 M0.46; its binding is negatively cooperative with a Hill coefficient of 0.46. Replacement of ferricyanide by the other components of the electron transport system yields hyperbolic kinetics with an apparent Km for D-lactate of 26 mM. The apparent Km for ferricyanide is 2.2 X 10(-4) M. Phosphate and pyrophosphate compounds stimulate the D-lactate:ferricyanide activity. These properties suggest that interaction of this enzyme with other electron transport proteins in the chain may enhance D-lactate binding and, hence, the rate of electron transport.
    Digital Access Access Options