engGoñi, GZoellner, ALisurek, MVelazquez-Campoy, APinto, SGomez-Moreno, CHannemann, FBernhardt, RMedina, M.Cyanobacterial Electron Carrier Proteins as Electron Donors to CYP106A2 from Bacillus Megaterium ATCC 13368ART-2009-64934The CYP450 from Bacillus megaterium (BmCYP106A2) catalyzes the 15βhydroxylation of several steroids and also synthesizes mono-hydroxylated 9α- and 11αOH-progesterone BmCYP106A2. The present study reports on the ability of BmCYP106A2 to be efficiently reduced by a truncated bovine adrenodoxin mutant, as well as 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, do not rely on a precise complementarity of the reacting molecules, rearrangements might be required and alternative binding modes might contribute to the observed ET reactions.2009http://zaguan.unizar.es/record/168483http://zaguan.unizar.es/record/168483oai:zaguan.unizar.es:168483Biochimica et Biophysica Acta - Proteins and Proteomics 1794, 11 (2009), 1635-1642by-nc-ndhttps://creativecommons.org/licenses/by-nc-nd/4.0/deed.esinfo:eu-repo/semantics/openAccess