The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase.

Abstract

Dihydroxy-acid dehydratase has been purified from Escherichia coli and characterized as a homodimer with a subunit molecular weight of 66,000. The combination of UV visible absorption, EPR, magnetic circular dichroism, and resonance Raman spectroscopies indicates that the native enzyme contains a [4Fe-4S]2+,+ cluster, in contrast to spinach dihydroxy-acid… (More)

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@article{Flint1993TheRA, title={The role and properties of the iron-sulfur cluster in Escherichia coli dihydroxy-acid dehydratase.}, author={David H. Flint and Mark H Emptage and Marybeth Finnegan and W. Fu and M. Kimo Johnson}, journal={The Journal of biological chemistry}, year={1993}, volume={268 20}, pages={14732-42} }