Mechanism of Cysteine Desulfurase Slr0387 from Synechocystis sp. PCC 6803:  Kinetic Analysis of Cleavage of the Persulfide Intermediate by Chemical Reductants

• Published in: Biochemistry (Easton) Vol. 43; no. 38; pp. 12220 - 12226
• Main Authors: Behshad, Elham, Parkin, Sara E, Bollinger, J. Martin
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 28.09.2004
• Subjects: Carbon-Sulfur Lyases - metabolism; Catalysis; Cyanobacteria - enzymology; Cysteine - metabolism; Dithiothreitol - pharmacology; Hydrogen-Ion Concentration; Kinetics; Mercaptoethanol - pharmacology; Phosphines - pharmacology; Pyridoxal Phosphate - pharmacology; Reducing Agents - chemistry; Reducing Agents - metabolism; Spectrum Analysis; Sulfhydryl Compounds - metabolism; Sulfides - chemistry; Sulfides - metabolism; Synechocystis; Temperature; USA, Washington

Cysteine desulfurases (CDs) are pyridoxal-5‘-phosphate (PLP)-dependent enzymes that cleave sulfur from cysteine via an enzyme cysteinyl persulfide intermediate. In vitro studies of these enzymes have generally employed dithiothreitol as a cosubstrate to reductively cleave the persulfide intermediate...