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      A soluble NADH dehydrogenase (NADH: ferricyanide oxidoreductase) from Thermus aquaticus strain T351.

      Walsh, K.A.; Daniel, Roy M.; Morgan, Hugh W.
      DOI
       http://www.biochemj.org/bj/209/bj2090427.htm
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      Walsh, K.A., Daniel, R.M. & Morgan, H.W. (1983). A soluble NADH dehydrogenase (NADH: ferricyanide oxidoreductase) from Thermus aquaticus strain T351. Biochemical Journal, 209(2), 427-433.
      Permanent Research Commons link: https://hdl.handle.net/10289/4518
      Abstract
      A soluble NADH dehydrogenase (NADH:ferricyanide oxidoreductase) has been obtained by simple disruption of cells of Thermus aquaticus strain T351, and purified. The enzyme is of low molecular mass, 50 000 Da, and displays many of the properties of the membrane-bound enzyme, including inhibition by both NADH and ferricyanide, and the same Km for ferricyanide. The enzyme contains 0.05 mol of FMN, 0.16 mol of labile sulphur and 2.2 mol of iron per mol of protein. The enzyme is inhibited by NAD and cupferron competitively with ferricyanide, and by ATP (but not ADP) competitively with NADH. The enzyme is particularly thermostable, having a half-life at 95 degrees C of 35 min. The effect of temperature on the molar absorption coefficient and the stability of NADH was determined.
      Date
      1983
      Type
      Journal Article
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      • Science and Engineering Papers [3122]
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