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Activation and reduction of carbon dioxide by nitrogenase iron proteins

Nature Chemical Biology volume 13, pages 147–149 (2017)Cite this article

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Abstract

The iron (Fe) proteins of molybdenum (Mo) and vanadium (V) nitrogenases mimic carbon monoxide (CO) dehydrogenase in catalyzing the interconversion between CO2 and CO under ambient conditions. Catalytic reduction of CO2 to CO is achieved in vitro and in vivo upon redox changes of the Fe-protein-associated [Fe4S4] clusters. These observations establish the Fe protein as a model for investigation of CO2 activation while suggesting its biotechnological adaptability for recycling the greenhouse gas into useful products.

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Figure 1: In vitro reduction of CO2 to CO by Fe proteins.
Figure 2: Interactions of CO2 and CO with the [Fe4S4] clusters of the Fe proteins.
Figure 3: In vivo reduction of CO2 to CO by Fe proteins.

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Acknowledgements

This work is supported by UCI startup funds and a Hellman Fellowship (to Y.H.).

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Authors and Affiliations

  1. Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, California, USA

    Johannes G Rebelein, Martin T Stiebritz, Chi Chung Lee & Yilin Hu

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  1. Johannes G Rebelein
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  2. Martin T Stiebritz
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  3. Chi Chung Lee
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  4. Yilin Hu
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Contributions

J.G.R., M.T.S. and C.C.L. performed experiments and analyzed data; Y.H. designed experiments, analyzed data and wrote the paper.

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Correspondence to Yilin Hu.

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The authors declare no competing financial interests.

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Supplementary Results, Supplementary Table 1 and Supplementary Figures 1–9. (PDF 1845 kb)

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Rebelein, J., Stiebritz, M., Lee, C. et al. Activation and reduction of carbon dioxide by nitrogenase iron proteins. Nat Chem Biol 13, 147–149 (2017). https://doi.org/10.1038/nchembio.2245

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