Stability of oxidized, reduced and copper bound forms of Bacillus subtilis Sco

Davidson, David E.; Hill, Bruce C.

doi:10.1016/j.bbapap.2008.10.005

Cited by 20 publications

(35 citation statements)

References 41 publications

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“…The B. subtilis Sco1 is implicated in formation of the Cu A site in CcO. The intriguing aspect of the Bacillus Sco1 is its dramatic preference for Cu(II) over Cu(I) (98). The marked stability of the Cu(II)-Sco1 complex may necessitate a conversion step to an intermediate state of Cu(I)-Sco1 compatible with Cu transfer (99).…”

Section: Copper Metallochaperones For Cytochrome Oxidasementioning

confidence: 99%

Copper Metallochaperones

Robinson

Winge

2010

Annu. Rev. Biochem.

655

530

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The current state of knowledge on how copper metallochaperones support the maturation of cuproproteins is reviewed. Copper is needed within mitochondria to supply the CuA and intramembrane CuB sites of cytochrome oxidase, within the trans-Golgi network to supply secreted cuproproteins and within the cytosol to supply superoxide dismutase 1 (Sod1). Subpopulations of copper-zinc superoxide dismutase also localize to mitochondria, the secretory system, the nucleus and, in plants, the chloroplast, which also requires copper for plastocyanin. Prokaryotic cuproproteins are found in the cell membrane and in the periplasm of gram-negative bacteria. Cu(I) and Cu(II) form tight complexes with organic molecules and drive redox chemistry, which unrestrained would be destructive. Copper metallochaperones assist copper in reaching vital destinations without inflicting damage or becoming trapped in adventitious binding sites. Copper ions are specifically released from copper metallochaperones upon contact with their cognate cuproproteins and metal transfer is thought to proceed by ligand substitution.

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Section: Copper Metallochaperones For Cytochrome Oxidasementioning

confidence: 99%

Copper Metallochaperones

Robinson

Winge

2010

Annu. Rev. Biochem.

655

530

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“…For example, the melting temperature ( T m ) of a copper metallochaperone BsSco was determined to increase by 23 °C when bound to Cu(II). 69 Ca(II) and Zn(II) ion binding to coagulation factors IX binding protein increased its melting temperature by 4–5 °C and calculated enthalpic parameter (Δ H cal ) by more than 100 kcal mol −1 . 70 The DSC results illustrate that metal bound α 3 DIV is more stable than its apo counterpart in thermally induced denaturations.…”

Section: Discussionmentioning

confidence: 99%

Apoprotein Structure and Metal Binding Characterization of a de Novo Designed Peptide, α₃DIV, that Sequesters Toxic Heavy Metals

Plegaria¹,

Dzul

Zuiderweg³

et al. 2015

Biochemistry

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De novo protein design is a biologically relevant approach that provides a novel process in elucidating protein folding and modeling the metal centers of metalloproteins in a completely unrelated or simplified fold. An integral step in de novo protein design is the establishment of a well-folded scaffold with one conformation, which is a fundamental characteristic of many native proteins. Here, we report the NMR solution structure of apo α3DIV at pH 7.0, a de novo designed three-helix bundle peptide containing a triscysteine motif (Cys18, Cys28, and Cys67) that binds toxic heavy metals. The structure comprises 1067 NOE restraints derived from multinuclear multidimensional NOESY, as well as 138 dihedral angles (ψ, φ, and χ1). The backbone and heavy atoms of the 20 lowest energy structures have a root mean square deviation from the mean structure of 0.79 (0.16) Å and 1.31 (0.15) Å, respectively. When compared to the parent structure α3D, the substitution of Leu residues to Cys enhanced the α-helical content of α3DIV while maintaining the same overall topology and fold. In addition, solution studies on the metalated species illustrated metal-induced stability. An increase in the melting temperatures was observed for Hg(II), Pb(II), or Cd(II) bound α3DIV by 18–24 °C compared to its apo counterpart. Further, the extended X-ray absorption fine structure analysis on Hg(II)-α3DIV produced an average Hg(II)–S bond length at 2.36 Å, indicating a trigonal T-shaped coordination environment. Overall, the structure of apo α3DIV reveals an asymmetric distorted triscysteine metal binding site, which offers a model for native metalloregulatory proteins with thiol-rich ligands that function in regulating toxic heavy metals, such as ArsR, CadC, MerR, and PbrR

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“…Such a redox transformation could be an important aspect of the copper transfer role proposed for BsSco in Cu A assembly [55]. Such a redox transformation could be an important aspect of the copper transfer role proposed for BsSco in Cu A assembly [55].…”

Section: Cumentioning

confidence: 90%

Metallochaperones - an Overview

Sekhon¹

2010

curr chem biol

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Improper allocation of the incorrect metal ion to a metalloprotein can have resounding and often detrimental effects on different aspects of cellular physiology. Enzymes that employ transition metals as co-factors are housed in a wide variety of intracellular locations or are exported to the extracellular milieu. Metallochaperones (much smaller than the cell) are essential for the proper functioning of cells and are a distinct class of proteins which accounts for the incorporation of metal ion cofactors into metalloenzymes / metalloproteins. Metals in the cells are distributed by metallochaperones (intracellular metal ion carriers) and these intracellular metal ion carriers ensure that the correct metal is acquired by a specific metalloenzyme. Metallochaperones act in the intracellular trafficking of metal ions to protect the cell and are a family of soluble metal receptor proteins that bind and protect metal ions/cofactors. The target sites for metal/cofactor delivery include a number of metalloenzymes, or proteins that bind metal ions and use these ions as cofactors to perform essential biochemical reactions such as cellular respiration, DNA synthesis and antioxidant defense. In this review, metallochaperones for various metals such as copper, nickel, zinc, iron, arsenic, manganese, cobalt, molybdenum and vanadium are discussed. In the cell, the specific metal ion is often selected by specific protein-protein interactions between the apoprotein and a metallochaperone and ligand-exchange reactions have been involved in the metal transfer from metallochaperones to cognate apoproteins. The development of chaperone-based medications from medicinal plants has been reported.

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Stability of oxidized, reduced and copper bound forms of Bacillus subtilis Sco

Cited by 20 publications

References 41 publications

Copper Metallochaperones

Copper Metallochaperones

Apoprotein Structure and Metal Binding Characterization of a de Novo Designed Peptide, α₃DIV, that Sequesters Toxic Heavy Metals

Metallochaperones - an Overview

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Stability of oxidized, reduced and copper bound forms of Bacillus subtilis Sco

Cited by 20 publications

References 41 publications

Copper Metallochaperones

Copper Metallochaperones

Apoprotein Structure and Metal Binding Characterization of a de Novo Designed Peptide, α3DIV, that Sequesters Toxic Heavy Metals

Metallochaperones - an Overview

Contact Info

Product

Resources

About

Apoprotein Structure and Metal Binding Characterization of a de Novo Designed Peptide, α₃DIV, that Sequesters Toxic Heavy Metals