The CYP450 from Bacillus megaterium (BmCYP106A2) catalyzes the 15beta-hydroxylation of several steroids and also synthesizes mono-hydroxylated 9alpha- and 11alpha-OH-progesterone. This study reports on the ability of BmCYP106A2 to be efficiently reduced by the photosynthetic flavodoxin and, particularly, ferredoxin electron carriers from the cyanobacterium Anabaena. These results open the possibility for the design of a hybrid system to provide reducing equivalents for the hydroxylation process. Additionally, they suggest that despite the interaction of BmCYP106A2 with these proteins, particularly with flavodoxin, they do not rely on a precise complementarity of the reacting molecules, rearrangements might be required and alternative binding modes might contribute to the observed electron transfer reactions.