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. 2007 Jun 15;104(26):11109–11114. doi: 10.1073/pnas.0611636104

Fig. 4.

Fig. 4.

Redox titration analysis (pH 7.9) of recombinant B4–GAPDH and eight different site-specific mutants of B subunits. Each form displayed about the same NADPH-dependent specific activity under fully reducing conditions (set to 1), except mutant R77A, whose maximal specific activity was 50% in respect to the other forms (22). Data of mutants R77A and E362Q are taken from ref. 22. When significant, data points were fitted to the Nernst equation and the midpoint redox potential was calculated (Em,7.9). (A) B4–GAPDH (Em,7.9 = −347 mV). (B) Mutants E362Q (open circles) and R183A (filled circles). (C) Mutants R191A (filled circles), E356/357Q (open circles), and R77A (triangles). (D) Mutants E356Q (triangles, Em,7.9 = −355 mV), E357Q (asterisks, Em,7.9 = −353 mV), and D351N (open circles, Em,7.9 = −345 mV). In B, C, and D, the redox titration curve of B4–GAPDH is shown as a broken line for comparison.