Cyanobacterial Electron Carrier Proteins as Electron Donors to CYP106A2 from Bacillus Megaterium ATCC 13368

Goñi, G ; Zoellner, A ; Lisurek, M ; Velazquez-Campoy, A (Universidad de Zaragoza) ; Pinto, S ; Gomez-Moreno, C (Universidad de Zaragoza) ; Hannemann, F ; Bernhardt, R ; Medina, M. (Universidad de Zaragoza)

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)