Correct assembly of iron-sulfur cluster fs0 into escherichia coli dimethyl sulfoxide reductase (dmsabc) is a prerequisite for molybdenum cofactor insertion*

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  • who: Huipo Tang from the Huipo Tang1, Richard ARothery, James E. Voss, and Joel H. Weiner, From the Department of Biochemistry, School of Molecular and Systems Medicine, University of Alberta, Edmonton, Alberta T G , Canada The , [ Fe- S] cluster of the catalytic subunit (DmsA) of Escherichia coli dimethyl sulfoxide reductase (DmsABC) plays a key role in the electron transfer relay. We have now established an additional role for the cluster in directing molybdenum cofactor assembly during enzyme maturation. EPR spectroscopy indicates that , has a high spin ground state (S ⴝ, ⁄2) in its reduced form, resulting in an . . .

     

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