The Peptidyl-Prolyl Isomerase Activity of SlyD Is Not Required for the Maturation of Escherichia coli Hydrogenase

Department of Chemistry, University of Toronto, Toronto, Ontario, Canada M5S 3H6

^* To whom correspondence should be addressed. Email: dzamble{at}chem.utoronto.ca.

	Abstract

Escherichia coli SlyD, which is involved in the biosynthesis of the metal cluster in the [NiFe]-hydrogenase enzymes, exhibits several activities including that of a peptidyl-prolyl isomerase (PPIase). Mutations that result in deficient PPIase activity do not produce a corresponding decrease in the other activities of SlyD in vitro or in hydrogenase production in vivo.