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Cyanobacterial electron carrier proteins as electron donors to CYP106A2 fromBacillus megateriumATCC 13368

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
1570-9639
Publisher
Elsevier
Publication Date
Volume
1794
Issue
11
Identifiers
DOI: 10.1016/j.bbapap.2009.07.012
Keywords
  • Cyp106A2
  • Adrenodoxin
  • Ferredoxin
  • Flavodoxin
  • Protein–Protein Interaction
  • Electron Transfer
  • Transient Interaction
Disciplines
  • Biology
  • Design

Abstract

Abstract The CYP450 from Bacillus megaterium ( BmCYP106A2) catalyzes the 15β-hydroxylation of several steroids and also synthesizes mono-hydroxylated 9α- and 11α-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.

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