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Figure 1 | BMC Biochemistry

Figure 1

From: Comparative thermodynamic studies on substrate and product binding of O-Acetylserine Sulfhydrylase reveals two different ligand recognition modes

Figure 1

Spectroscopic characterization of OASS and ligand binding. (A) Fluorescence emission of OASS upon excitation at 295 nm and quenching of fluorescence due to ligand binding (down arrow indicates decrease in fluorescence upon addition of ligands). (B) Fluorescence emission of OASS upon excitation at 412 nm (PLP) and change in fluorescence intensity due to methionine binding (upward arrow indicates increase in PLP fluorescence upon addition of ligands). Fluorescence increase at 507 nm was used for determining the extent of binding. (C) Cartoon representation of substrate (OAS), substrate analogue (methionine), and product (cysteine) used in this study.

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