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, Bethany G; Bastin, Baback; Yang, Chen; Neubauer, Thomas J; Young, Robert P; Hilario, Eduardo; Huang, Yu-ming M; Chang, Chia-en A; Fan, Li; Dunn, Michael F; Marsella, Michael J; Mueller, Leonard J

Caulkins, Bethany G; Bastin, Baback; Yang, Chen; Neubauer, Thomas J; Young, Robert P; Hilario, Eduardo; Huang, Yu-ming M; Chang, Chia-en A; Fan, Li; Dunn, Michael F; Marsella, Michael J; Mueller, Leonard J.

Affiliation

Caulkins BG; Department of Chemistry, University of California , Riverside, California 92521, United States.

J Am Chem Soc ; 136(37): 12824-7, 2014 Sep 17.

Article in En | MEDLINE | ID: mdl-25148001

Subject(s)

Protons; Pyridoxal Phosphate/chemistry; Salmonella typhimurium/enzymology; Schiff Bases/chemistry; Tryptophan Synthase/chemistry; Catalytic Domain; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Pyridoxal Phosphate/metabolism; Salmonella typhimurium/chemistry; Salmonella typhimurium/metabolism; Schiff Bases/metabolism; Tryptophan Synthase/metabolism

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Full text: 1 Database: MEDLINE Main subject: Protons / Pyridoxal Phosphate / Salmonella typhimurium / Schiff Bases / Tryptophan Synthase Language: En Journal: J Am Chem Soc Year: 2014 Type: Article Affiliation country: United States

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