Showing papers by "Eduardo A. Ceccarelli published in 1993"

TL;DR: Results indicated that aromaticity is the most important factor to the function of the tyrosine in catalysis when the mutants were assayed for cytochrome c reduction, indicating that the presence of the phenol ring at the carboxyl-terminal position of wild-type reductase is important, but not an absolute requirement for enzyme function or FAD assembly.

TL;DR: The purified transgenic enzyme showed kinetic and spectroscopic properties that were similar to those reported for the plant flavoprotein, indicating that, even when fused to the 27-kDa transferase portion, the reductase was still able to assemble FAD and to acquire an active conformation in the bacterial host.