Resumen: The 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. Idioma: Inglés Año: 2009 Publicado en: Biochimica et Biophysica Acta - Proteins and Proteomics 1794, 11 (2009), 1635-1642 ISSN: 1570-9639 Factor impacto JCR: 2.48 (2009) Categ. JCR: BIOPHYSICS rank: 41 / 74 = 0.554 (2009) - Q3 - T2 Categ. JCR: BIOCHEMISTRY & MOLECULAR BIOLOGY rank: 153 / 281 = 0.544 (2009) - Q3 - T2 Tipo y forma: Article (PostPrint) Área (Departamento): Área Bioquímica y Biolog.Mole. (Dpto. Bioq.Biolog.Mol. Celular)