Format

Send to

Choose Destination
FEBS Lett. 2005 Sep 26;579(23):5236-40.

Role of conserved cysteines in mediating sulfur transfer from IscS to IscU.

Author information

1
Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602, USA.

Abstract

The role of the three conserved cysteine residues on Azotobacter vinelandii IscU in accepting sulfane sulfur and forming a covalent complex with IscS has been evaluated using electrospray-ionization mass spectrometry studies of variants involving individual cysteine-to-alanine substitutions. The results reveal that IscS can transfer sulfur to each of the three alanine-substituted forms of IscU to yield persulfide or polysulfide species, and formation of a heterodisulfide covalent complex between IscS and Cys(37) on IscU. It is concluded that S transfer from IscS to IscU does not involve a specific cysteine on IscU or the formation of an IscS-IscU heterodisulfide complex.

PMID:
16165131
PMCID:
PMC1360219
DOI:
10.1016/j.febslet.2005.08.046
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Wiley Icon for PubMed Central
Loading ...
Support Center