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Warui, D. M., Li, N., Nørgaard, H., Krebs, C., Bollinger, J. M., Jr., Booker, S. J. Detection of formate, rather than carbon monoxide, as the stoichiometric coproduct in conversion of fatty aldehydes to alkanes by a cyanobacterial aldehyde decarbonylase. J. Am. Chem. Soc., 2011, 133, 3316–3319.
Arcinas, A. J., Booker, S. J. Radical break-up, blissful make-up. Nat. Chem. Biol., 2011, 7, 133–134.
Grove, T. L., Benner, J. S., Radle, M. I., Ahlum, J. H., Landgraf, B. J., Krebs, C., Booker, S. J. A radically different mechanism for S-adenosylmethionine-dependent methyltransferases. Science, 2011, 332, 604–607.
Li, N., Nørgaard, H., Warui, D. M., Booker, S. J., Krebs, C., Bollinger, J. M., Jr, Conversion of fatty aldehydes to alka(e)nes and formate by a cyanobacterial aldehyde decarbonylase: Cryptic redox by an unusual dimetal oxygenase. J. Am. Chem. Soc., 2011, 133, 6158–6161
Boal, A. K., Grove, T. L., McLaughlin, M. I., Yennawar, N., Booker, S. J., Rosenzweig, A. C. Structural basis for methyl transfer by a radical SAM enzyme. Science, 2011, 332, 1089–1092.
Grove, T. L., Radle, M. I., Krebs, C., Booker, S. J. Cfr and RlmN contain a single [4Fe–4S] cluster, which directs two distinct reactivities for S-adenosylmethionine: methyl transfer by SN2 displacement and radical generation. J. Am. Chem. Soc., 2011, 133, 19586–19589.
Krebs, C.*, Bollinger, J. M., Jr.*, Booker, S. J.* "Cyanobacterial alkane biosynthesis expands the functional and mechanistic repertoire of the "di-iron-carboxylate" proteins," Current Opinion Chem. Biol., 2011, 15, 291-303.
Grove, T. L., Ahlum, J. H., Sharma, P., Krebs, C., Booker, S. J. "A consensus mechanism for radical SAM-dependent dhydrogenation? BtrN contains two [4fe-FS] clusters," Biochemistry, 2010, 49, 3783-3785.
Booker, S. J. "Anaerobic functionalization of unactivated C–H bonds," Curr. Opin. Chem. Biol., 2009, 13, 58–73
Saleh, L., Lee, K.-H., Anton, B. P., Madinger, C. L., Benner, J. S. Roberts, R. J. Krebs, C. and Booker, S. J. "Characterization of RimO, a new member of the methylthioltransferase subclass of the radical SAM superfamily," Biochemistry, 2009, 48, 10162–10174.
Matthews, M. L., Neumann, C. S., Miles, L. A., Grove, T. L., Booker, S. J., Krebs, C., Walsh, C. T., Bollinger, J. M. Jr. "Substrate positioning controls the partition between halogenation and hydroxylation in the aliphatic halogenase, SyrB2," Proc. Natl. Acad. Sci. USA, 2009, 106, 17723–17728.
Saunders, A. H., Griffiths, A. E., Lee, K.-H., Cicchillo, R. M., Tu, L. Stromberg, J. A., Krebs, C., and Booker, S. J. "Characterication of quinolinate synthases from Escherichia coli, Mycobacterium tuberculosis, and Pyrococcus horikoshii indicates that [4Fe-4S] clusters are common cofactors throughout this class of enzymes," Biochemistry, 2008, 47, 10999-1012
Chatterjee, A., Li, S., Zhang, Y., Grove, T. L., Lee, M., Krebs, C., Booker, S. J., Begley, T. P., Ealick, S. E. "Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily," Nat. Chem. Biol., 2008, 4, 758-765