Binding of Cu(II) or Zn(II) in a de novo designed triple‐stranded <i>α</i>‐helical coiled‐coil toward a prototype for a metalloenzyme

Kiyokawa, Tomohiro; Kanaori, Kenji; Tajima, Kunihiko; Koike, Mitsumasa; Mizuno, Toshihisa; Oku, Jun-ichi; Tanaka, Toshiki

doi:10.1111/j.1399-3011.2004.00109.x

Cited by 42 publications

(58 citation statements)

References 42 publications

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“…An area of particular interest has been the introduction of metal-binding sites into the hydrophobic interiors of α-helical bundles and coiled coils. Examples of single metal ions that can be incorporated into coiled coils and helical bundles include heme centers [4] and mononuclear complexes of Zn 2+ [5][6][7][8], Cu 2+ [6,9,10], Cu + [11], Ni 2+ [10], Cd 2+ [12][13][14][15][16][17][18][19][20], Hg 2+ [12,14,16,17,[20][21][22][23][24][25][26], As 3+ [17,20,[26][27][28], Pb 2+ [18,20,29], and Bi 3+ [18]. Given these notable successes, the introduction of multinuclear metal complexes into synthetic proteins presents another challenging target to pursue.…”

Section: Introductionmentioning

confidence: 99%

Metal-binding properties and structural characterization of a self-assembled coiled coil: Formation of a polynuclear Cd–thiolate cluster

Zaytsev

Morozov

Fan

et al. 2013

Journal of Inorganic Biochemistry

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Section: Introductionmentioning

confidence: 99%

Metal-binding properties and structural characterization of a self-assembled coiled coil: Formation of a polynuclear Cd–thiolate cluster

Zaytsev

Morozov

Fan

et al. 2013

Journal of Inorganic Biochemistry

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“…Examples of Cu(I) (13,14) and Cu(II) de novo designed helix bundles have been reported (15)(16)(17)(18)(19)(20)(21)(22)(23)(24). However, only a few examples of controlled binding of copper at (His) 3 sites are known (17,20,21).…”

Section: +mentioning

confidence: 99%

“…However, only a few examples of controlled binding of copper at (His) 3 sites are known (17,20,21). Although Cu(I)/(II) redox processes were presented for a few systems (13,14,22), none was fully characterized in both oxidation states, which is essential for catalytic copper redox protein designs.…”

Section: +mentioning

confidence: 99%

Designing a functional type 2 copper center that has nitrite reductase activity within α-helical coiled coils

Tegoni

Yu²,

Bersellini

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

101

188

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One of the ultimate objectives of de novo protein design is to realize systems capable of catalyzing redox reactions on substrates. This goal is challenging as redox-active proteins require design considerations for both the reduced and oxidized states of the protein. In this paper, we describe the spectroscopic characterization and catalytic activity of a de novo designed metallopeptide Cu(I/II)(TRIL23H) 3 +/2+ , where Cu(I/II) is embeded in α-helical coiled coils, as a model for the Cu T2 center of copper nitrite reductase. In Cu(I/II)(TRIL23H) 3 +/2+ , Cu(I) is coordinated to three histidines, as indicated by X-ray absorption data, and Cu(II) to three histidines and one or two water molecules. Both ions are bound in the interior of the three-stranded coiled coils with affinities that range from nano- to micromolar [Cu(II)], and picomolar [Cu(I)]. The Cu(His) 3 active site is characterized in both oxidation states, revealing similarities to the Cu T2 site in the natural enzyme. The species Cu(II)(TRIL23H) 3 2+ in aqueous solution can be reduced to Cu(I)(TRIL23H) 3 + using ascorbate, and reoxidized by nitrite with production of nitric oxide. At pH 5.8, with an excess of both the reductant (ascorbate) and the substrate (nitrite), the copper peptide Cu(II)(TRIL23H) 3 2+ acts as a catalyst for the reduction of nitrite with at least five turnovers and no loss of catalytic efficiency after 3.7 h. The catalytic activity, which is first order in the concentration of the peptide, also shows a pH dependence that is described and discussed.

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“…Numerous peptide models have been examined to define and potentially replicate the native functional roles of metal ions within defined polypeptide structural contexts [40][41][42][43][44][45]. One of the most striking observations to emerge from these studies is the ability of metal ions to induce conformational transitions from the unfolded to folded state [46][47][48][49][50][51][52] or between different folded states [53][54][55] through interaction with the side chains of appropriately placed amino acid ligands within the polypeptide backbone. Moreover, metal ions can influence the supramolecular assembly of diseaserelated protein fibrils [56,57], either enhancing or inhibiting the process, depending on the stereoelectronic properties of the specific metal.…”

Section: Metal-ion-binding Sites In Peptides and Proteinsmentioning

confidence: 99%

Engineering responsive mechanisms to control the assembly of peptide-based nanostructures

Dublin

Zimenkov

Conticello

2009

Biochemical Society Transactions

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Complex biological machines arise from self-assembly on the basis of structural features programmed into sequence-specific macromolecules (i.e. polypeptides and polynucleotides) at the molecular level. As a consequence of the near-absolute control of macromolecular architecture that results from such sequence specificity, biological structural platforms may have advantages for the creation of functional supramolecular assemblies in comparison with synthetic polymers. Thus biological structural motifs present an attractive target for the synthesis of artificial nanoscale systems on the basis of relationships between sequence and supramolecular structure that have been established for native biological assemblies. In the present review, we describe an approach to the creation of structurally defined supramolecular assemblies derived from synthetic alpha-helical coiled-coil structural motifs. Two distinct challenges are encountered in this approach to materials design: the ability to recode the canonical sequences of native coiled-coil structural motifs to accommodate the formation of structurally defined supramolecular assemblies (e.g. synthetic helical fibrils) and the development of methods to control supramolecular self-assembly of these peptide-based materials under defined conditions that would be amenable to conventional processing methods. In the present review, we focus on the development of mechanisms based on guest-host recognition to control fibril assembly/disassembly. This strategy utilizes the latent structural specificity encoded within sequence-defined peptides to couple a conformational transition within the coiled-coil motifs to incremental changes in environmental conditions. The example of a selective metal-ion-induced conformational switch will be employed to validate the design principles.

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Binding of Cu(II) or Zn(II) in a de novo designed triple‐stranded α‐helical coiled‐coil toward a prototype for a metalloenzyme

Cited by 42 publications

References 42 publications

Metal-binding properties and structural characterization of a self-assembled coiled coil: Formation of a polynuclear Cd–thiolate cluster

Metal-binding properties and structural characterization of a self-assembled coiled coil: Formation of a polynuclear Cd–thiolate cluster

Designing a functional type 2 copper center that has nitrite reductase activity within α-helical coiled coils

Engineering responsive mechanisms to control the assembly of peptide-based nanostructures

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