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Journal of Bacteriology, April 2007, p. 2941-2944, Vol. 189, No. 7
0021-9193/07/$08.00+0     doi:10.1128/JB.01200-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Biosynthesis of the Thioquinolobactin Siderophore: an Interesting Variation on Sulfur Transfer{triangledown}

Amy M. Godert,1 Mi Jin,2 Fred W. McLafferty,2 and Tadhg P. Begley2*

Department of Biological and Chemical Sciences, Wells College, Aurora, New York 13026,1 Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 148532

Received 2 August 2006/ Accepted 21 December 2006

The thioquinolobactin siderophore from Pseudomonas fluorescens ATCC 17400 utilizes a variation of the sulfur transfer chemistry found in thiamine and molydobterin biosynthesis. A JAMM motif protein cleaves the C-terminal amino acid residues following a diglycine moiety on a small sulfur carrier protein, and the modified C terminus is activated and sulfurylated, forming a thiocarboxylate.

* Corresponding author. Mailing address: Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853. Phone: (607) 255-7133. Fax: (607) 255-4137. E-mail: tpb2{at}cornell.edu.

{triangledown} Published ahead of print on 5 January 2007.

Journal of Bacteriology, April 2007, p. 2941-2944, Vol. 189, No. 7
0021-9193/07/$08.00+0     doi:10.1128/JB.01200-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.





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