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The iron–sulfur‐containing HypC‐HypD scaffold complex of the NiFe‐hydrogenase maturation machinery is an ATPase
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The iron–sulfur‐containing HypC‐HypD scaffold complex of the NiFe‐hydrogenase maturation machinery is an ATPase
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Journal Article
The iron–sulfur‐containing HypC‐HypD scaffold complex of the NiFe‐hydrogenase maturation machinery is an ATPase
2019
Overview
HypD and HypC, or its paralogue HybG in Escherichia coli, form the core of the scaffold complex that synthesizes the Fe(CN)2CO component of the bimetallic NiFe‐cofactor of [NiFe]‐hydrogenase. We show here that purified HypC‐HypD and HybG‐HypD complexes catalyse hydrolysis of ATP to ADP (kcat ≅ 0.85·s−1); the ATPase activity of the individual proteins was between 5‐ and 10‐fold lower than that of the complex. Pre‐incubation of HypD with ATP was necessary to restore full activity upon addition of HybG. The conserved Cys41 residue on HypD was essential for full ATPase activity of the complex. Together, our data suggest that HypD undergoes ATP‐dependent conformational activation to facilitate complex assembly in preparation for substrate reduction. The iron–sulfur protein HypD and the small HypC chaperone form the core of the [NiFe]‐hydrogenase maturation machinery. We report here that both proteins have intrinsic ATP‐hydrolyzing activity and that this activity is synergistically enhanced in the HypD‐HypC complex. Our results support a model whereby HypD undergoes ATP‐dependent conformational activation, which allows manifestation of optimal ATPase activity upon HypC binding.
Publisher
John Wiley & Sons, Inc,John Wiley and Sons Inc,Wiley
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