De Novo Design of a Cytochrome<i>b</i>Maquette for Electron Transfer and Coupled Reactions on Electrodes

Chen, Xiaoxi; Discher, Bohdana M.; Pilloud, Denis L.; Gibney, Brian R.; Moser, Christopher C.; Dutton, P. Leslie

doi:10.1021/jp012185h

Cited by 44 publications

(54 citation statements)

References 50 publications

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“…22,38–40 De novo protein design has shown that the exterior of the helix bundle can be tailored with specific patterns of charge or hydrophobicity so as to facilitate insertion into vesicles, orientation at interfaces, or assembly on solid substrates, while preserving the interior of the helix bundle, that is, its designed functionality. 37,41–44 …”

Section: Resultsmentioning

confidence: 99%

New Design of Helix Bundle Peptide−Polymer Conjugates

et al. 2008

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We present a new design of peptide–polymer conjugates where a polymer chain is covalently linked to the side chain of a helix bundle-forming peptide. The effect of conjugated polymer chains on the peptide structure was examined using a de novo designed three-helix bundle and a photoactive four-helix bundle. Upon attachment of poly(ethylene glycol) to the exterior of the coiled-coil helix bundle, the peptide secondary structure was stabilized and the tertiary structure, that is, the coiled-coil helix bundle, was retained. When a heme-binding peptide as an example is used, the new peptide–polymer conjugate architecture also preserves the built-in functionalities within the interior of the helix bundle. It is expected that the conjugated polymer chains act to mediate the interactions between the helix bundle and its external environment. Thus, this new peptide–polymer conjugate design strategy may open new avenues to macroscopically assemble the helix bundles and may enable them to function in nonbiological environments.

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Section: Resultsmentioning

confidence: 99%

New Design of Helix Bundle Peptide−Polymer Conjugates

et al. 2008

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“…Gooding and associates have addressed aspects of this comprehensive area focusing on electrode-protein contacts via carbon nanotube contacts [28,29]. Still another novel aspect of bioelectrochemistry and protein film voltammetry is related to interfacial electrochemistry of totally synthetic proteins, particularly synthetic 4-α-helix-bundle heme proteins as developed by Dutton [30], Willner [31], Haehnel [32] and their associates. This area of design and synthesis of functional electron transfer and catalytic proteins parallels the introduction of novel physical electrochemistry, particularly in situ scanning tunnelling microscopy (in situ STM) in bioelectrochemistry, cf.…”

Section: Introductionmentioning

confidence: 99%

Voltammetry and Electrocatalysis of Achromobacter Xylosoxidans Copper Nitrite Reductase on Functionalized Au(111)-Electrode Surfaces

Welinder¹,

Zhang²,

Hansen³

et al. 2007

Zeitschrift Für Physikalische Chemie

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A long-standing issue in protein film voltammetry (PFV), particularly electrocatalytic voltammetry of redox enzyme monolayers, is the variability of protein adsorption modes, reflected in distributions of catalytic activity of the adsorbed protein/enzyme molecules. Use of well-defined, atomically planar electrode surfaces is a step towards the resolution of this central issue.We report here the voltammetry of copper nitrite reductase (CNiR, Achromobacter xylosoxidans) on Au(111)-electrode surfaces modified by monolayers of a broad variety of thiol-based linker molecules. These represent positively charged and electrostatically neutral, hydrophobic and hydrophilic, aliphatic and aromatic, and variable-length microenvironments, as well as their combinations. Optimal conditions for enzyme function seems to be a combination of hydrophobic and hydrophilic surface linker properties, which can lead to close to complete non-catalytic monolayer interfacial electron transfer function and electrocatalysis with activity approaching enzyme activity in homogeneous solution. Thiophenol (combined hydrophobic stacking and interdispersed water molecules), 4-methyl-thiophenol (hydrophobic and water molecules), and 3-and 4-aminothiophenol * Corresponding author. E-mail: ju@kemi.dtu.dk 1344 A. C. Welinder et al.(hydrophilic, hydrophobic) offer the overall most efficient micro-environments. Subtle differences with even small structural linker differences, however, lead to widely different electrocatalytic properties, strikingly illuminated by the ω-mercaptoamines. CuNiR thus shows highly efficient, close to ideal reversible electrocatalytic voltammetry on cysteaminecovered Au(111)-electrode surfaces, most likely due to two cysteamine orientations previously disclosed by in situ scanning tunnelling microscopy. Such a dual orientation exposes both a hydrophobic and a positively charged, hydrophilic surface feature. In contrast, the higher cysteamine homologues expose only the hydrophilic component with no electrocatalytic activity on these surfaces. These results offer a basis for rational surface design in forthcoming biological electrocatalysis useful both fundamentally and in novel biosensor technology.

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“…Furthermore, maquettes are designed to be environmentally robust to foster the development of biochemical devices for technological applications ranging from driving catalytic redox reactions to biosensors and bioremediation. By adapting the pattern of amino acid charges on the maquette surface, the interaction with electrode surfaces and therefore the electron transfer to/from the maquettes can be readily controlled 4. However, previous surface electrochemical studies of protein maquettes have been constrained to planar electrodes4, 5 and the monolayer surface densities of self‐adsorbed maquettes provide only small, milliOD (OD, optical density units) spectroscopic signals.…”

Section: Introductionmentioning

confidence: 99%

Functionalizing Nanocrystalline Metal Oxide Electrodes With Robust Synthetic Redox Proteins

Topoglidis¹,

Discher

Moser

et al. 2003

ChemBioChem

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De novo designed synthetic redox proteins (maquettes) are structurally simpler, working counterparts of natural redox proteins. The robustness and adaptability of the maquette protein scaffold are ideal for functionalizing electrodes. A positive amino acid patch has been designed into a maquette surface for strong electrostatic anchoring to the negatively charged surfaces of nanocrystalline, mesoporous TiO(2) and SnO(2) films. Such mesoporous metal oxide electrodes offer a major advantage over conventional planar gold electrodes by facilitating formation of high optical density, spectroelectrochemically active thin films with protein loading orders of magnitude greater (up to 8 nmol cm(-2)) than that achieved with gold electrodes. The films are stable for weeks, essentially all immobilized-protein display rapid, reversible electrochemistry. Furthermore, carbon monoxide ligand binding to the reduced heme group of the protein is maintained, can be sensed optically and reversed electrochemically. Pulsed UV excitation of the metal oxide results in microsecond or faster photoreduction of an immobilized cytochrome and millisecond reoxidation. Upon substitution of the heme-group Fe by Zn, the light-activated maquette injects electrons from the singlet excited state of the Zn protoporphyrin IX into the metal oxide conduction band. The kinetics of cytochrome/metal oxide interfacial electron transfer obtained from the electrochemical and photochemical data obtained are discussed in terms of the free energies of the observed reactions and the electronic coupling between the protein heme group and the metal oxide surface.

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De Novo Design of a CytochromebMaquette for Electron Transfer and Coupled Reactions on Electrodes

Cited by 44 publications

References 50 publications

New Design of Helix Bundle Peptide−Polymer Conjugates

New Design of Helix Bundle Peptide−Polymer Conjugates

Voltammetry and Electrocatalysis of Achromobacter Xylosoxidans Copper Nitrite Reductase on Functionalized Au(111)-Electrode Surfaces

Functionalizing Nanocrystalline Metal Oxide Electrodes With Robust Synthetic Redox Proteins

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