ArticleBiochemistry2013
Metal transfer within the Escherichia coli HypB-HypA complex of hydrogenase accessory proteins.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- The HypA and HypB metallochaperones from Methanococcus maripaludis have unique metal-binding properties and a distinct nickel transfer mechanism.The Journal of biological chemistry · 2026Article
- Structural investigations connect the disordered N-terminal extension of HypB to the activities of HypB and SlyD in E. coli.Protein science : a publication of the Protein Society · 2025Article
- Selective inhibition of NikA mediated Ni(II) import in E. coli by the Indium(III)-EDTA complex.Metallomics : integrated biometal science · 2025Article
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Moving metals: How microbes deliver metal cofactors to metalloproteins.Molecular microbiology · 2023Article
- Promising approaches for the assembly of the catalytically active, recombinant Desulfomicrobium baculatum hydrogenase with substitutions at the active site.Microbial cell factories · 2023Article
- Selective Turn-On Fluorescence Sensing of Cyanide Using the Pyridoxal Platform of a Ni(II) Complex.ACS omega · 2022Article
- The role of nucleoside triphosphate hydrolase metallochaperones in making metalloenzymes.Metallomics : integrated biometal science · 2022Review
- Revealing potential functions of hypothetical proteins induced by genistein in the symbiosis island of Bradyrhizobium japonicum commercial strain SEMIA 5079 (= CPAC 15).BMC microbiology · 2022Article
- COG0523 proteins: a functionally diverse family of transition metal-regulated G3E P-loop GTP hydrolases from bacteria to man.Metallomics : integrated biometal science · 2021Article
- Mechanistic Insights into the Metal-Dependent Activation of ZnInorganic chemistry · 2019Article
- Bimodal Nickel-Binding Site onInorganic chemistry · 2019Article
- A whole-cell, high-throughput hydrogenase assay to identify factors that modulate [NiFe]-hydrogenase activity.The Journal of biological chemistry · 2019Article
- Nickel Metalloregulators and Chaperones.Inorganics · 2019Article
- pH Dependent Reversible Formation of a Binuclear NiInorganics · 2019Article
- High-affinity metal binding by the Escherichia coli [NiFe]-hydrogenase accessory protein HypB is selectively modulated by SlyD.Metallomics : integrated biometal science · 2017Article
- Metallochaperones and metalloregulation in bacteria.Essays in biochemistry · 2017Review
- CO synthesized from the central one-carbon pool as source for the iron carbonyl in O2-tolerant [NiFe]-hydrogenase.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Anaerobic Formate and Hydrogen Metabolism.EcoSal Plus · 2016Review
- Distribution of Hydrogenases in Cyanobacteria: A Phylum-Wide Genomic Survey.Frontiers in genetics · 2016Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The maturation of [NiFe]-hydrogenase in Escherichia coli is a complex process involving many steps and multiple accessory proteins. The two accessory proteins HypA and HypB interact with each other and are thought to cooperate to insert nickel into the active site of the hydrogenase-3 precursor protein. Both of these accessory proteins bind metal individually, but little is known about the metal-binding activities of the proteins once they assemble together into a functional complex. In this study, we investigate how complex formation modulates metal binding to the E. coli proteins HypA and HypB. This work lead to a re-evaluation of the HypA nickel affinity, revealing a KD on the order of 10(-8) M. HypA can efficiently remove nickel, but not zinc, from the metal-binding site in the GTPase domain of HypB, a process that is less efficient when complex formation between HypA and HypB is disrupted. Furthermore, nickel release from HypB to HypA is specifically accelerated when HypB is loaded with GDP, but not GTP. These results are consistent with the HypA-HypB complex serving as a transfer step in the relay of nickel from membrane transporter to its final destination in the hydrogenase active site and suggest that this complex contributes to the metal fidelity of this pathway.
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