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Imaging active site chemistry and protonation states: NMR crystallography of the tryptophan synthase α-aminoacrylate intermediate.
Holmes JB, Liu V, Caulkins BG, Hilario E, Ghosh RK, Drago VN, Young RP, Romero JA, Gill AD, Bogie PM, Paulino J, Wang X, Riviere G, Bosken YK, Struppe J, Hassan A, Guidoulianov J, Perrone B, Mentink-Vigier F, Chang CA, Long JR, Hooley RJ, Mueser TC, Dunn MF, Mueller LJ. Holmes JB, et al. Among authors: caulkins bg. Proc Natl Acad Sci U S A. 2022 Jan 11;119(2):e2109235119. doi: 10.1073/pnas.2109235119. Proc Natl Acad Sci U S A. 2022. PMID: 34996869 Free PMC article.
Protonation states of the tryptophan synthase internal aldimine active site from solid-state NMR spectroscopy: direct observation of the protonated Schiff base linkage to pyridoxal-5'-phosphate.
Caulkins BG, Bastin B, Yang C, Neubauer TJ, Young RP, Hilario E, Huang YM, Chang CE, Fan L, Dunn MF, Marsella MJ, Mueller LJ. Caulkins BG, et al. J Am Chem Soc. 2014 Sep 17;136(37):12824-7. doi: 10.1021/ja506267d. Epub 2014 Sep 3. J Am Chem Soc. 2014. PMID: 25148001 Free PMC article.
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