Open AccessStructural domains in NADPH: Protochlorophyllide oxidoreductases involved in catalysis and substrate binding. Final report
Author(s) -
Michael P. Timko
Publication year - 1999
Language(s) - English
Resource type - Reports
DOI - 10.2172/766046
Subject(s) - protochlorophyllide , cofactor , thylakoid , substrate (aquarium) , plastid , chemistry , substrate specificity , biochemistry , function (biology) , catalysis , enzyme , biophysics , biology , microbiology and biotechnology , oxidoreductase , chloroplast , ecology , gene
Until recently little direct information was available about specific structural determinants within the light-dependent NADPH: protochlorophyllide oxidoreductases (PORs) required for substrate and cofactor binding, catalytic activity, and thylakoid membrane localization. Based on our previous DOE-funded studies, during the past year we brought to fruition a number of ongoing experiments, initiated several new avenues of investigations, and overall have made considerable progress towards establishing the basic structural parameters governing POR function. Our studies to date have defined residues and domains involved in substrate and cofactor binding and catalysis, and elaborated on the mechanism for membrane localization of POR in developing plastids. Our results and their significance, as well as our work in progress, are detailed