Combining a Nitrogenase Scaffold and a Synthetic Compound into an Artificial Enzyme |
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| Authors: | Dr Kazuki Tanifuji Dr Chi Chung Lee Prof?Dr Yasuhiro Ohki Prof?Dr Kazuyuki Tatsumi Prof?Dr Yilin Hu Prof?Dr Markus W Ribbe |
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| Institution: | 1. Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA 92697‐3900 (USA);2. Department of Chemistry, Graduate School of Science and Research Center for Materials Science, Nagoya University, Furo‐cho, Chikusa‐ku, Nagoya 464‐8602 (Japan);3. Department of Chemistry, University of California, Irvine, Irvine, CA 92697‐2025 (USA) |
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| Abstract: | Nitrogenase catalyzes substrate reduction at its cofactor center ((Cit)MoFe7S9C]n?; designated M‐cluster). Here, we report the formation of an artificial, nitrogenase‐mimicking enzyme upon insertion of a synthetic model complex (Fe6S9(SEt)2]4?; designated Fe6RHH) into the catalytic component of nitrogenase (designated NifDKapo). Two Fe6RHH clusters were inserted into NifDKapo, rendering the conformation of the resultant protein (designated NifDKFe) similar to the one upon insertion of native M‐clusters. NifDKFe can work together with the reductase component of nitrogenase to reduce C2H2 in an ATP‐dependent reaction. It can also act as an enzyme on its own in the presence of EuIIDTPA, displaying a strong activity in C2H2 reduction while demonstrating an ability to reduce CN? to C1–C3 hydrocarbons in an ATP‐independent manner. The successful outcome of this work provides the proof of concept and underlying principles for continued search of novel enzymatic activities based on this approach. |
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| Keywords: | artificial enzyme nitrogenase synthetic compound C C coupling hydrocarbon |
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