| Literature DB >> 16165131 |
Archer D Smith1, Jeverson Frazzon, Dennis R Dean, Michael K Johnson.
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.Entities:
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Year: 2005 PMID： 16165131 PMCID： PMC1360219 DOI： 10.1016/j.febslet.2005.08.046
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124