Abstract
Quantitative EPR data on frozen reaction mixtures of NADPH with free FAD and with chloroplast NADP + reductase respectively show that the fraction of the flavin moiety of the enzyme which exists in the radical form is at least 100 times larger than that of free FAD under identical conditions. It is concluded that the apoenzyme stabilize the radical form of the bound flavin and thereby facilitate electron transfer from chlorophyll to NADP +.
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