Sulfur mobilization in cyanobacteria: the catalytic mechanism of L-cystine C-S lyase (C-DES) from synechocystis.

Abstract

Sulfur mobilization represents one of the key steps in ubiquitous Fe-S clusters assembly and is performed by a recently characterized set of proteins encompassing cysteine desulfurases, assembly factors, and shuttle proteins. Despite the evolutionary conservation of these proteins, some degree of variability among organisms was observed, which might reflect functional specialization. L-Cyst(e)ine lyase (C-DES), a pyridoxal 5'-phosphatedependent enzyme identified in the cyanobacterium Synechocystis, was reported to use preferentially cystine over cysteine with production of cysteine persulfide, pyruvate, and ammonia. In this study, we demonstrate that C-DES sequences are present in all cyanobacterial genomes and constitute a new family of sulfur-mobilizing enzymes, distinct from cysteine desulfurases. The functional properties of C-DES from Synechocystis sp. PCC 6714 were investigated under pre-steady-state and steady-state conditions. Single wavelength and rapid scanning stopped-flow kinetic data indicate that the internal aldimine reacts with cystine forming an external aldimine that rapidly decays to a transient quinonoid species and stable tautomers of the alpha-aminoacrylate Schiff base. In the presence of cysteine, the transient formation of a dipolar species precedes the selective and stable accumulation of the enolimine tautomer of the external aldimine, with no formation of the alpha-aminoacrylate Schiff base under reducing conditions. Effective sulfur mobilization from cystine might represent a mechanism that allows adaptation of cyanobacteria to different environmental conditions and to light-dark cycles.

• Authors: Barbara Campanini, Francesca Schiaretti, Stefania Abbruzzetti, Dorothea Kessler, Andrea Mozzarelli
• Journal: The Journal of biological chemistry (J Biol Chem) Vol. 281 Issue 50 Pg. 38769-80 (Dec 15 2006) ISSN: 0021-9258 [Print] United States
• PMID: 17020883 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Sulfur
• Carbon-Sulfur Lyases
• L-cysteine-cystine C-S lyase

Topics

• Amino Acid Sequence
• Carbon-Sulfur Lyases (chemistry, metabolism)
• Catalysis
• Molecular Sequence Data
• Sequence Homology, Amino Acid
• Spectrophotometry, Ultraviolet
• Sulfur (metabolism)
• Synechocystis (metabolism)