TY  - JOUR
A1  - Colas, Helene
A1  - Ewen, Kerstin M.
A1  - Hannemann, Frank
A1  - Bistolas, Nikitas
A1  - Wollenberger, Ursula
A1  - Bernhardt, Rita
A1  - de Oliveira, Pedro
T1  - Direct and mediated electrochemical response of the cytochrome P450 106A2 from Bacillus megaterium ATCC 13368
JF  - Bioelectrochemistry : an international journal devoted to electrochemical aspects of biology and biological aspects of electrochemistry ; official journal of the Bioelectrochemical Society
N2  - CYP106A2 is one of only a few known steroid hydroxylases of bacterial origin, which might be interesting for biotechnological applications. Despite the enzyme having been studied for more than 30 years, its physiological function remains elusive. To date, there have been no reports of the redox potential of CYP106A2, which was supposed to be unusually low for a cytochrome P450. In this work we show that cyclic voltammetry is not only suitable to determine the redox potential of challenging proteins such as CYP106A2, measured at - 128 mV vs. NHE, but also to study molecular interactions of the enzyme with different interaction partners via the respective electrochemical responses. The effect of small ligands, such as carbon monoxide and cyanide, was observed on the cyclic voltammograms of CYP106A2. Furthermore, we found that Tween 80 caused a positive shift of the redox potential of immobilised CYP106A2 indicative for water expulsion from the haem environment. Moreover, electron transfer mediation phenomena with biological redox partners (e.g. ferredoxins) were studied. Finally, the influence of two different kinds of substrates on the electrochemical response of CYP106A2 was assessed, aligning observations from spectral and electrochemical studies.
KW  - Cytochrome P450
KW  - Cyclic voltammetry
KW  - Modified electrode
KW  - Protein interaction
KW  - Substrate binding
Y1  - 2012
U6  - https://doi.org/10.1016/j.bioelechem.2012.01.006
SN  - 1567-5394
VL  - 87
IS  - 5
SP  - 71
EP  - 77
PB  - Elsevier
CY  - Lausanne
ER  -