Effects of axial ligand mutation of the type I copper site in bilirubin oxidase on direct electron transfer-type bioelectrocatalytic reduction of dioxygen

Kamitaka, Yuji; Tsujimura, Seiya; Kataoka, Keisuke; Sakurai, Takeshi; Ikeda, Tokuji; Kano, Kenji

doi:10.1016/j.jelechem.2006.10.035

Cited by 106 publications

(100 citation statements)

References 33 publications

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“…The electrochemistry of the Met → Gln mutant of bilirubin oxidase indicated that the intramolecular electron transfer between the type I copper center and the trinuclear copper center were accelerated as expected from the change in redox potential [84]. The electric current density due to the electron transfer between the electrode surface and type I copper of fungal laccases [80,82], bilirubin oxidase [81,84] and CueO [83] dramatically increased in the presence of dioxygen, since dioxygen was effectively converted to water without forming activated oxygen species. CueO was found to be the most promising cathodic catalyst to construct a biofuel cell because of high stability and high electric current density.…”

Section: Function Of Type I Copper In Multicopper Oxidasesmentioning

confidence: 93%

“…The redox potential of type I copper in some MCOs has also been measured electrochemically [79][80][81][82][83][84], although a molecular mass higher than 50 kDa is exceptionally unfavorable for obtaining clear electrochemical responses. Direct electrochemistry using pyrolytic graphite as a working electrode or mediated electrochemistry using Au electrodes modified with an appropriate promoter by self assembly permit the measurement of the redox potential of type I copper, when the MCO molecules take the appropriate orientation on the electrode surface and electric communication between the electrode and type I copper becomes possible.…”

Section: Properties Of Type I Copper In Multicopper Oxidasesmentioning

confidence: 99%

“…Direct electrochemistry using pyrolytic graphite as a working electrode or mediated electrochemistry using Au electrodes modified with an appropriate promoter by self assembly permit the measurement of the redox potential of type I copper, when the MCO molecules take the appropriate orientation on the electrode surface and electric communication between the electrode and type I copper becomes possible. Thus, the redox potential of the type I coppers of plant and fungal laccases [80], ascorbate oxidase [79], bilirubin oxidase [81,84], CeuO [83] have been electrochemically determined, although the association of these proteins and the electrode sometimes gave slightly different values from those determined by the titration method. The shorter the distance of type I copper from the protein surface, the better the electrochemical response.…”

Section: Properties Of Type I Copper In Multicopper Oxidasesmentioning

confidence: 99%

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Structure and function of type I copper in multicopper oxidases

Sakurai

Kataoka

2007

Cell. Mol. Life Sci.

132

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Abstract. The type I copper center in multicopper oxidases is constructed from 1Cys2His and weakly coordinating 1Met or the non-coordinating 1Phe/1Leu, and it exhibits spectral properties and an alkaline transition similar to those of the blue copper center in blue copper proteins. Since the type I copper center in multicopper oxidases is deeply buried inside the protein molecule, electron transfers to and from type I copper are performed through specific pathways: the hydrogen bond between an amino acid located at the substrate binding site and a His residue coordinating type I copper, and the His-Cys-His sequence connecting the type I copper center and the trinuclear copper center comprised of a type II copper and a pair of type III coppers. The intramolecular electron transfer rates can be tuned by mutating the fourth ligand of type I copper. Further, mutation at the Cys ligand gives a vacant type I copper center and traps the reaction intermediate during the four-electron reduction of dioxygen.

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Section: Function Of Type I Copper In Multicopper Oxidasesmentioning

confidence: 93%

Section: Properties Of Type I Copper In Multicopper Oxidasesmentioning

confidence: 99%

Section: Properties Of Type I Copper In Multicopper Oxidasesmentioning

confidence: 99%

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Structure and function of type I copper in multicopper oxidases

Sakurai

Kataoka

2007

Cell. Mol. Life Sci.

132

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“…[44][45][46][47] A mutant of Myrothecium verrucaria (Mv) BOD, displaying a lower Cu T1 redox potential, was however shown to catalyze O 2 reduction at a lower poten- CHEMELECTROCHEM REVIEWS www.chemelectrochem.org tial than the wild type. [48] This suggests that the electrode can be recognized as the primary electron donor to the MCOs, and can provide direct access to the potential values for the T1 Cu centers (Table 1). [41,47,[49][50][51][52][53] The Cu II /Cu I transition of the T1 center for plant and fungal LACs are determined to be between + 0.22 and + 0.58 V vs. Ag/AgCl.…”

Section: Enzymes For O 2 Reductionmentioning

confidence: 98%

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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“…MCOs such as CueO (copper efflux oxidase) from Escherichia coli [4][5][6] and bilirubin oxidase (BOD) from Myrothecium verrucaria [7] have been extensively studied at the aims of revealing their structure-function relationships and applying them to cathodic enzymes for biofuel cell and clinical test [8][9][10]. [16,17] or by performing the mutation at the Met ligand for T1Cu in BOD to Gln [18].…”

Section: Introductionmentioning

confidence: 99%

Study on dioxygen reduction by mutational modifications of the hydrogen bond network leading from bulk water to the trinuclear copper center in bilirubin oxidase

Morishita

Kurita

Kataoka

et al. 2014

Biochemical and Biophysical Research Communications

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Bilirubin oxidase is a multicopper oxidase containing a type I Cu center to specifically oxidize bilirubin and related substrates and a trinuclear Cu center to perform four-electron reduction of dioxygen as the final electron acceptor. Special attentions have been paid on multicopper oxidases, since this class of enzymes has potential uses as electrocatalyst for biofuel cells and biosensor and catalyst to form a variety of dyes. In addition, bilirubin oxidase has been utilized for the clinical test of liver. In spite of wide attention and potential wide use of the enzyme, structural and functional studies on bilirubin oxidase have been limited.The present study is on the proton transfer mechanism for dioxygen reduction by bilirubin oxidase. We performed mutation at Glu463 located in the hydrogen bond network leading from bulk water to the active site deeply buried inside protein molecule. By singly performing mutation at this amino acid and doubly performing mutation at a Cys ligand to type I Cu center in addition to the mutation at Glu463, we could trap two reaction intermediates, and characterized them in comparisons with those trapped in other multicopper oxidases.We believe this study attracts wide attention from researches studying on biochemistry, bioinorganic chemistry, electrochemistry, biophysics and related fields including bioinspired chemistry, and contributes in the understanding of the four-electron reduction by multicopper oxidases and more widely, transport of protons in protein molecules. According to reasons as above we would like to publish our results in the world wide BBRC. sincerely yours, Takeshi Sakurai Cover LetterProton transport pathway in bilirubin oxidase was mutated Two intermediates in the dioxygen reduction steps were trapped and characterized.A specific glutamate for dioxygen reduction by multicopper oxidases was identified.

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Effects of axial ligand mutation of the type I copper site in bilirubin oxidase on direct electron transfer-type bioelectrocatalytic reduction of dioxygen

Cited by 106 publications

References 33 publications

Structure and function of type I copper in multicopper oxidases

Structure and function of type I copper in multicopper oxidases

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

Study on dioxygen reduction by mutational modifications of the hydrogen bond network leading from bulk water to the trinuclear copper center in bilirubin oxidase

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Effects of axial ligand mutation of the type I copper site in bilirubin oxidase on direct electron transfer-type bioelectrocatalytic reduction of dioxygen

Cited by 106 publications

References 33 publications

Structure and function of type I copper in multicopper oxidases

Structure and function of type I copper in multicopper oxidases

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

Study on dioxygen reduction by mutational modifications of the hydrogen bond network leading from bulk water to the trinuclear copper center in bilirubin oxidase

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