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Catalytic Activities of NifEN: Implications for Nitrogenase Evolution and Mechanism
Yilin Hu, Janice M. Yoshizawa, Aaron W. Fay, Chi Chung Lee, Jared A. Wiig, Markus W. Ribbe and Douglas C. Rees
Proceedings of the National Academy of Sciences of the United States of America
Vol. 106, No. 40 (Oct. 6, 2009), pp. 16962-16966
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/40485119
Page Count: 5
You can always find the topics here!Topics: Electrons, Catalysis, Enzymes, Biochemistry, Electron transfer, Molecular evolution, Azotobacter vinelandii, Catalytic activity, Spectroscopy, Skeleton
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NifEN is a key player in the biosynthesis of nitrogenase MoFe protein. It not only shares a considerable degree of sequence homology with the MoFe protein, but also contains clusters that are homologous to those found in the MoFe protein. Here we present an investigation of the catalytic activities of NifEN. Our data show that NifEN is catalytically competent in acetylene (C ₂ H ₂ ) and azide (NJ) reduction, yet unable to reduce dinitrogen (N ₂ ) or evolve hydrogen (H ₂ ). Upon turnover, C ₂ H₂ gives rise to an additional 5 = 1/2 signal, whereas NJ perturbs the signal originating from the NifEN-associated FeMoco homolog. Combined biochemical and spectroscopic studies reveal that NJ can act as either an inhibitor or an activator for the binding and/or reduction of C ₂ H₂/while carbon monoxide (CO) is a potent inhibitor for the binding and/or reduction of both NJ and C ₂ H₂ . Taken together, our results suggest that NifEN is a catalytic homolog of MoFe protein; however, it is only a "skeleton" version of the MoFe protein, as its associated clusters are simpler in structure and less versatile in function, which, in turn, may account for its narrower range of substrates and lower activities of substrate reduction. The resemblance of NifEN to MoFe protein in catalysis points to a plausible, sequential appearance of the two proteins in nitrogenase evolution. More importantly, the discrepancy between the two systems may provide useful insights into nitrogenase mechanism and allow reconstruction of a fully functional nitrogenase from the "skeleton" enzyme, NifEN.
Proceedings of the National Academy of Sciences of the United States of America © 2009 National Academy of Sciences