The kinetic mechanism of the SufC ATPase: The cleavage step is accelerated by SufB

doi:10.1074/jbc.M513455200

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Papers In Press, published online ahead of print January 23, 2006
J. Biol. Chem, 10.1074/jbc.M513455200
Submitted on December 19, 2005
Revised on January 18, 2006
Accepted on January 23, 2006

The kinetic mechanism of the SufC ATPase: The cleavage step is accelerated by SufB

John F. Eccleston, Arsen Petrovic, Colin T. Davis, Kaveri Rangachari, and Robert J. M. (Iain) Wilson

Physical Biochemistry, National Institute for Medical Research, London NW7 1AA

Corresponding Author: jeccles{at}nimr.mrc.ac.uk

Protein products of the suf operon are involved in iron-sulfur metabolism. SufC is an ATPase which 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 slow cleavage of mantATP to mantADP and the release of Pi. 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,C proteins interact and how the SufB,C proteins interact in the processes involved in regulating iron-sulfur transfer.

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