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J. Biol. Chem., Vol. 281, Issue 13, 8371-8378, March 31, 2006

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The Kinetic Mechanism of the SufC ATPase

THE CLEAVAGE STEP IS ACCELERATED BY SufB^*

From the Medical Research Council National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, United Kingdom

Protein products of the suf operon are involved in iron-sulfur metabolism. SufC is an ATPase that can interact with SufB in the absence of nucleotide. We have studied the transient kinetics of the SufC ATPase mechanism using the fluorescent ATP analogue, 2'(3')-O-N-methylanthraniloyl-ATP (mantATP). mantATP initially binds to SufC weakly. A conformational change of the SufC·mantATP complex then occurs followed by the very slow cleavage of mantATP to mantADP and the rapid release of P_i. In the presence of SufB, the cleavage step is accelerated and the release of mantADP is inhibited. Both of these effects promote the formation of a SufC·mantADP complex. In the absence and presence of SufB, mantADP remains more tightly bound to SufC than mantATP. These studies provide a basis for how the SufB and -C proteins interact in the processes involved in regulating iron-sulfur transfer.

Received for publication, November 18, 2005 , and in revised form, January 23, 2006.

^* The work was supported by the Medical Research Council, UK. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Tel.: 44-208-959-3666; Fax: 44-208-906-4477; E-mail jeccles{at}nimr.mrc.ac.uk.

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