Direct electrochemistry of cytochrome bo3 oxidase at a series of gold nanoparticles-modified electrodes

Melin, Frédéric; Meyer, Thomas; Lankiang, Styven; Choi, Sung-Soon; Gennis, Robert B.; Blanck, Christian; Schmutz, Marc; Hellwig, Petra

doi:10.1016/j.elecom.2012.10.024

Cited by 20 publications

(20 citation statements)

References 27 publications

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“…The technique is based on porous three‐dimensional gold nanoparticle electrodes obtained by drop‐casting a concentrated gold colloid on the surface of a polycrystalline gold substrate. These electrodes allow both an exceptionally high surface coverage and a reversible direct electron transfer with the immobilized enzyme [22–24]. After immobilization of CcO, the catalytic current and the oxygen reduction potential can be investigated in presence of oxygen [23].…”

Section: Introductionmentioning

confidence: 99%

Electrochemistry suggests proton access from the exit site to the binuclear center in Paracoccus denitrificans cytochrome c oxidase pathway variants

Meyer

Melin

Richter³

et al. 2015

FEBS Letters

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a b s t r a c tTwo different pathways through which protons access cytochrome c oxidase operate during oxygen reduction from the mitochondrial matrix, or the bacterial cytoplasm. Here, we use electrocatalytic current measurements to follow oxygen reduction coupled to proton uptake in cytochrome c oxidase isolated from Paracoccus denitrificans. Wild type enzyme and site-specific variants with defects in both proton uptake pathways (K354M, D124N and K354M/D124N) were immobilized on gold nanoparticles, and oxygen reduction was probed electrochemically in the presence of varying concentrations of Zn 2+ ions, which are known to inhibit both the entry and the exit proton pathways in the enzyme. Our data suggest that under these conditions substrate protons gain access to the oxygen reduction site via the exit pathway.

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Section: Introductionmentioning

confidence: 99%

Electrochemistry suggests proton access from the exit site to the binuclear center in Paracoccus denitrificans cytochrome c oxidase pathway variants

Meyer

Melin

Richter³

et al. 2015

FEBS Letters

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“…In comparison, cco with a His-tag on subunit I did not show any direct electrocatalytic behavior in similar ptBLM assemblies, which again emphasizes the importance of protein orientation. We have recently shown that oxidases immobilized on 15 nm gold NPs modified with a mixture of hexane thiol and 6-mercapto-1-hexanol also exhibit a clear electrocatalytic activity in presence of oxygen, see Figure 3 (Melin et al , 2013 ). Larger NPs mediate the electron transfer less efficiently.…”

Section: Terminal Oxidasesmentioning

confidence: 99%

“…In a preliminary study, our group has shown that gold NPs constitute an efficient support for the immobilization of several respiratory membrane proteins fragments from the thermophilic bacterium Thermus thermophilus (Meyer et al , 2011 ). The immobilization of full terminal oxidases on gold NPs is now possible (Melin et al , 2013 ).…”

Section: Mixed Protein/nanomaterials Filmsmentioning

confidence: 99%

Recent advances in the electrochemistry and spectroelectrochemistry of membrane proteins

Melin

Hellwig

2013

Biological Chemistry

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Abstract:Integral membrane proteins are encountered in fundamental natural processes, such as photosynthesis and respiration. The relation between the structure of the proteins and their function and dynamics are still not clear in most cases. Once fully understood, these processes could ultimately help researchers to develop alternative methods for producing energy, either from light or biomass. They could also lead to more efficient antibiotics, which would selectively inhibit a specific membrane protein of pathogenic bacteria. Since the chemical reactions involved in both photosynthesis and respiration are redox reactions, electrochemical methods can play a considerable role in uncovering their mechanisms. The electrochemical characterization of membrane proteins is, however, quite challenging. An overview on the techniques used for the characterization of membrane proteins, including classical approaches such as voltammetry and spectroelectrochemistry, and recent developments, such as their combination with surface-enhanced techniques is given.

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“…[328][329][330] Immobilization of these enzymes on electrodes is a challenge, however, because it requires sophisticated modification of the electrode mimic of the cell membrane. [331,332] Moreover, many of the terminal oxidases currently reported reduce oxygen at a much lower potential than MCOs. [333] Some bacterial metabolisms in the biodiversity pool are known to involve high-potential electron-transfer chains.…”

Section: Chemelectrochem Reviewsmentioning

confidence: 99%

Biohydrogen for a New Generation of H₂/O₂ Biofuel Cells: A Sustainable Energy Perspective

et al. 2014

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Among sustainable alternatives to fossil fuel, proton exchange membrane fuel cells are promising devices that deliver electricity from hydrogen and oxygen, producing only water. The transformation of the fuel and oxidant however relies on rare‐metal catalysts. H2/O2 enzymatic biofuel cells thus emerge as sustainable biotechnological devices in which chemical catalysts are replaced by hydrogenases at the anode and multicopper oxidases at the cathode. This review discusses the recent breakthroughs and the limitations in all the components of H2/O2 biofuel cells: 1) Catalytic mechanisms involved in multicopper oxidases and hydrogenases, in addition to the new potential of enzymes from the biodiversity pool, which exhibit outstanding properties. 2) The molecular basis for oriented enzyme immobilization on the electrochemical interfaces as a prerequisite for a fast direct electron‐transfer rate. 3) The requirement for 3D networks to enhance current densities. 4) The production of H2 from biomass. 5) The history of H2/O2 biofuel cells and recent devices, which also highlights the remaining issues that will allow the use of such devices in low‐power applications.

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Direct electrochemistry of cytochrome bo3 oxidase at a series of gold nanoparticles-modified electrodes

Cited by 20 publications

References 27 publications

Electrochemistry suggests proton access from the exit site to the binuclear center in Paracoccus denitrificans cytochrome c oxidase pathway variants

Electrochemistry suggests proton access from the exit site to the binuclear center in Paracoccus denitrificans cytochrome c oxidase pathway variants

Recent advances in the electrochemistry and spectroelectrochemistry of membrane proteins

Biohydrogen for a New Generation of H₂/O₂ Biofuel Cells: A Sustainable Energy Perspective

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Direct electrochemistry of cytochrome bo3 oxidase at a series of gold nanoparticles-modified electrodes

Cited by 20 publications

References 27 publications

Electrochemistry suggests proton access from the exit site to the binuclear center in Paracoccus denitrificans cytochrome c oxidase pathway variants

Electrochemistry suggests proton access from the exit site to the binuclear center in Paracoccus denitrificans cytochrome c oxidase pathway variants

Recent advances in the electrochemistry and spectroelectrochemistry of membrane proteins

Biohydrogen for a New Generation of H2/O2 Biofuel Cells: A Sustainable Energy Perspective

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Product

Resources

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Biohydrogen for a New Generation of H₂/O₂ Biofuel Cells: A Sustainable Energy Perspective