Show simple item record  

dc.contributor.authorWalsh, K.A.
dc.contributor.authorDaniel, Roy M.
dc.contributor.authorMorgan, Hugh W.
dc.date.accessioned2010-09-02T22:54:51Z
dc.date.available2010-09-02T22:54:51Z
dc.date.issued1983
dc.identifier.citationWalsh, 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.en_NZ
dc.identifier.urihttps://hdl.handle.net/10289/4518
dc.description.abstractA 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.en_NZ
dc.language.isoen
dc.subjectbiologyen_NZ
dc.titleA soluble NADH dehydrogenase (NADH: ferricyanide oxidoreductase) from Thermus aquaticus strain T351.en_NZ
dc.typeJournal Articleen_NZ
dc.identifier.doihttp://www.biochemj.org/bj/209/bj2090427.htmen_NZ


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record