Wursteris blue

FIGURE 6. The reduction of oxidised Ba-MDH by endogenous substrate. MDH lacking any metal ion in its active site was produced from the mxaA mutant it was incubated with Ba + to produce Ba-MDH which was then oxidised with a small excess of Wursteris Blue which was then removed by rapid gel filtration and spectra recorded. Reproduced with permission from Goodwin and Anthony (1996), Biochemical Journal, 318, 673n679). the Biochemical Society. 

The oxidation state was eonfirmed by demonstrating that its isolated pros-thetie group was predominantly in the oxidised (quinone form). Figure 6 shows the speetrum of the Ba-MDH after oxidation at 4 C with a 1.5-fold excess of Wursteris Blue at pH 9. The speetrum of the initial oxidised form of the enzyme is very similar to that seen in Figure 4. 

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