Trafficking in persulfides: delivering sulfur in biosynthetic pathways.

Eugene G Mueller

Journal: Nature chemical biology 2006;2(4):185-94

PMID: 16547481

Full Text on Nature Publishing Group View on PubMed

Abstract

The presence of sulfur in cofactors has been appreciated for over a century, but the trafficking and delivery of sulfur to cofactors and nucleosides is still not fully understood. In the last decade, great strides have been made toward understanding those processes and the enzymes that conduct them, including cysteine desulfurases and rhodanese homology domain proteins. The persulfide group (R-S-SH) predominantly serves as the sulfur donor, and sulfur incorporation pathways share enzymes to a remarkable degree. Mechanisms for the use of persulfide groups are illustrated with the relatively simple case of 4-thiourdine generation, and further possibilities are illuminated by the 2-thiouridine and cofactor biosynthetic systems. The rationale and ramifications of sharing enzymes between sulfur incorporation pathways are discussed, including implications for interpreting genetic or genomic data that indicate a role for a sulfur transfer protein in a particular biological process.

Address: Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716, USA. [email protected]

DOI: 10.1038/nchembio779

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MeSH Terms: Alanine, Carbon-Sulfur Lyases, Disulfides, Escherichia coli, Escherichia coli Proteins, Iron-Sulfur Proteins, Models, Biological, Models, Chemical, Models, Genetic, Protein Binding, Protein Structure, Tertiary, Selenium, Sulfides, Sulfur, Sulfurtransferases, Thiamine, Thiosulfate Sulfurtransferase