The iron–sulfur‐containing HypC‐HypD scaffold complex of the [NiFe]‐hydrogenase maturation machinery is an ATPase

FEBS Open Bio

Kerstin Nutschan¹  R. Gary Sawers¹  Ralph P. Golbik² 

[1] Institute for Biology/Microbiology Martin‐Luther University Halle‐Wittenberg Germany;Institute of Biochemistry and Biotechnology Martin‐Luther University Halle‐Wittenberg Germany;

关键词: [NiFe]‐hydrogenase;    HybG;    HypC chaperone;    HypD;    iron–sulfur cluster;    metalloenzyme maturation;   

DOI  :  10.1002/2211-5463.12743

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown