Crystal Structure of the ATP-Dependent Maturation Factor of Ni,Fe-Containing Carbon Monoxide Dehydrogenases

Jeoung, Jae‐Hun; Giese, Till; Grünwald, Marlene; Dobbek, Holger

doi:10.1016/j.jmb.2009.12.062

Cited by 38 publications

(46 citation statements)

References 62 publications

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“…The participation of metalbinding NTPases in the biosynthetic pathways of complex metallocenters is an emerging trend (30), although whether a common theme of metal-regulated NTP hydrolysis exists is not yet clear. For example, metal-dependent dimerization was observed for CooC (28,29), the ATPase involved in carbon monoxide dehydrogenase biosynthesis, but ATP hydrolysis was not dramatically affected by the addition of nickel. Furthermore, the GTPase dedicated to urease maturation, UreG, binds nickel or zinc with micromolar affinities at a site that likely includes the CxH motif found at a similar location with respect to the GTPase motifs as C106/H107 of HpHypB (5,70,71).…”

Section: Discussionmentioning

confidence: 99%

Effects of Metal on the Biochemical Properties of Helicobacter pylori HypB, a Maturation Factor of [NiFe]-Hydrogenase and Urease

2011

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The biosyntheses of the [NiFe]-hydrogenase and urease enzymes in Helicobacter pylori require several accessory proteins for proper construction of the nickel-containing metallocenters. The hydrogenase accessory proteins HypA and HypB, a GTPase, have been implicated in the nickel delivery steps of both enzymes. In this study, the metal-binding properties of H. pylori HypB were characterized, and the effects of metal binding on the biochemical behavior of the protein were examined. The protein can bind stoichiometric amounts of Zn(II) or Ni(II), each with nanomolar affinity. Mutation of Cys106 and His107, which are located between two major GTPase motifs, results in undetectable Ni(II) binding, and the Zn(II) affinity is weakened by 2 orders of magnitude. These two residues are also required for the metal-dependent dimerization observed in the presence of Ni(II) but not Zn(II). The addition of metals to the protein has distinct impacts on GTPase activity, with zinc significantly reducing GTP hydrolysis to below detectable levels and nickel only slightly altering the k cat and K m of the reaction. The regulation of HypB activities by metal binding may contribute to the maturation of the nickel-containing enzymes.

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Section: Discussionmentioning

confidence: 99%

Effects of Metal on the Biochemical Properties of Helicobacter pylori HypB, a Maturation Factor of [NiFe]-Hydrogenase and Urease

2011

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“…Fe Incorporation into Cfd1 and Nbp35 in Vivo-For 55 Fe labeling experiments the genes encoding the Cfd1 or Nbp35 nucleotide binding and cysteine mutants were subcloned into the yeast vector pRS416-MET25 or pRS424-TDH3 (31) containing an N-terminal 3HA or a C-terminal TAP-tag sequence, respectively (32). In vivo radiolabeling of transformed yeast cells with 55 FeCl 3 and measurement of 55 Fe incorporation into 3HA or TAP-tagged Cfd1 and Nbp35 via anti-HA agarose or IgG-Sepharose immunoprecipitation was carried out as described (33).…”

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confidence: 99%

“…In vivo radiolabeling of transformed yeast cells with 55 FeCl 3 and measurement of 55 Fe incorporation into 3HA or TAP-tagged Cfd1 and Nbp35 via anti-HA agarose or IgG-Sepharose immunoprecipitation was carried out as described (33).…”

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confidence: 99%

A Bridging [4Fe-4S] Cluster and Nucleotide Binding Are Essential for Function of the Cfd1-Nbp35 Complex as a Scaffold in Iron-Sulfur Protein Maturation

Netz

Pierik

Stümpfig

et al. 2012

Journal of Biological Chemistry

119

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Background:The P-loop NTPases Cfd1 and Nbp35 form a scaffold complex for cytosolic-nuclear Fe-S cluster synthesis. Results: Two C-terminal cysteine residues of each Cfd1 and Nbp35 assemble a transient [4Fe-4S] cluster in a nucleotide-dependent fashion. Conclusion:The results suggest a bridging nature of the transient [4Fe-4S] cluster of Cfd1-Nbp35. Significance: This study defines the molecular role of the Cfd1-Nbp35 tetrameric scaffold complex in Fe-S cluster assembly.

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“…Overexpression systems for the CODHs in E. coli, as with metalloproteins in general, have met with limited success due to the complexity of maturation process that is required to assemble the activity center. 5,6) Recently, the expression system for cooS II gene encoding CODH II from C. hydrogenoformans in E. coli was reported. 7,8) Notably, recombinant CODH II (Rec-CODH II) shows CO oxidation activity nearly equal to native CODH II.…”

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confidence: 99%

A Simple, Large-Scale Overexpression Method of Deriving Carbon Monoxide Dehydrogenase II from Thermophilic BacteriumCarboxydothermus hydrogenoformans

Inoue¹,

Yoshida²,

Wada³

et al. 2011

Bioscience, Biotechnology, and Biochemistry

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Crystal Structure of the ATP-Dependent Maturation Factor of Ni,Fe-Containing Carbon Monoxide Dehydrogenases

Cited by 38 publications

References 62 publications

Effects of Metal on the Biochemical Properties of Helicobacter pylori HypB, a Maturation Factor of [NiFe]-Hydrogenase and Urease

Effects of Metal on the Biochemical Properties of Helicobacter pylori HypB, a Maturation Factor of [NiFe]-Hydrogenase and Urease

A Bridging [4Fe-4S] Cluster and Nucleotide Binding Are Essential for Function of the Cfd1-Nbp35 Complex as a Scaffold in Iron-Sulfur Protein Maturation

A Simple, Large-Scale Overexpression Method of Deriving Carbon Monoxide Dehydrogenase II from Thermophilic BacteriumCarboxydothermus hydrogenoformans

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