Surface-Binding Peptide Facilitates Electricity-Driven NADPH-Free Cytochrome P450 Catalysis
Sarah Zernia, Ronny Frank, Renato H.-J. Weiße, Heinz-Georg Jahnke, Kathrin Bellmann-Sickert, Andrea Prager, Bernd Abel, Norbert Sträter, Andrea Robitzki, Annette G. Beck-Sickinger
Index: 10.1002/cctc.201800092
Full Text: HTML
Abstract
Abstract The front cover artwork for issue 3/2018 is a collaboration between three groups of Leipzig University and the Leibniz Institute of Surface Modification e.V., Leipzig (B. Abel). The university groups of A. Beck-Sickinger and A. Robitzki are from the Institute of Biochemistry and N. Sträter is a member of the Institute of Bioanalytical Chemistry. The image displays the immobilization of cytochrome P450 BM3 on metal oxides mediated by a binding peptide, which enables the energization of the enzyme with electric potential to facilitate electrocatalysis on different substrates. See the Full Paper itself at https://doi.org/10.1002/cctc.201701810. “A recombinant fusion of an indium tin oxide binding peptide and the multi-domain class VIII cytochrome P450 BM3 enable a direct electron supply. This approach is also feasible for pharmaceutical application.” This and more about the story behind the research featured on the front cover can be found in this issue's Cover Profile. Read the full text of the corresponding research at https://doi.org/10.1002/cctc.201701810.