The Reversible Change in the Redox State of Type I Cu in<i>Myrothecium verrucaria</i>Bilirubin Oxidase Depending on pH

Zoppellaro, Giorgio; Sakurai, Nobuo; Kataoka, Keisuke; Sakurai, Takeshi

doi:10.1271/bbb.68.1998

Cited by 13 publications

(8 citation statements)

References 12 publications

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“…Therefore, all these results of the EPR spectra indicate that not only was Pc autoreduced, but the new EPR signal with the larger hyperfine splitting reversibly emerged. It has been reported that the blue Cu center of Pc [10] and type I Cu of laccase [8] and bilirubin oxidase [9] are autoreduced at highly alkaline pHs. Therefore, at highly alkaline pHs, Pc is in an equilibrium of the three forms, the Cu(II) form, the form giving the new EPR signal and the form not giving the EPR spectrum.…”

Section: Resultsmentioning

confidence: 99%

The alkaline transition of blue copper proteins, Cucumis sativus plastocyanin and Pseudomonas aeruginosa azurin

Sakurai¹

2006

FEBS Letters

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Autoreduction of Cucumis sativus plastocyanin and Pseudomonas aeruginosa azurin took place at alkaline pHs, having been accompanied by the decrease in the intensities of the charge transfer band, Cys-S-(π)→Cu(II) at 597 and 626 nm, and the Cu(II)-EPR signals with small AII values of 6.5 x 10-3 and 5.3 x 10-3 cm-1 for plastocyanin and azurin, respectively. Further, an extra Cu(II)-EPR signal with a large AII value of 21 x 10-3 cm-1 also reversibly emerged with increasing pH. Plastocyanin and azurin are in an equilibrium of the three forms at alkaline pHs Dear Professor Richard Cogdell Editor FEBS LettersThank you very much for your suggestion to tidy us some of English before to submit the revised manuscript to FEBS Letters (FEBSLETTERS-S-05-01041R1). English was polished up by the professional English correction service as follows.About twenty "the" and "a' were deleted or added (not indicated).About fifteen commas were added (not indicated).Every "pH's" was converted to "pHs".Single form was changed to plural form and vice versa for some points.Other alterations are as follows. P2. Line 3: "has not been known" was change to "has not been hitherto understood". P2. Line 16: "solved" was deleted.P2. Line 17: "that" which had been deleted in the original manuscript was added.P2. Line 23 and others: "high alkaline pH's" was changed to "highly alkaline pHs". P3. Line 3: "till" was changed to "until".P3. Results and discussion, Lines 7 and 11 The order of words were changed from "slightly shifted" to "shifted slightly" and "in only" to "only in".P3. Line 5 from bottom: "with the spin Hamiltonian parameters" was added after "signal" and "typical to" was changed to "typical of". P4. Line 6: "recovered as that" was changed to "recovered to the level of that". P4. Line 11: "not only Pc was reduced" was changed to "not only was Pc reduced,". P4. Line 17: "the form to give" was changed to "the form giving". P4. Line 18: "In order to ascertain that" was converted to "In order to ascertain whether". P5. Line 21: "As conclusion" was changed to "In conclusion". P5. Line 3 from bottom: "under study" was changed to "being studied as to".Titles of cited papers were checked to be correct. Sincerely yours, Takeshi Sakurai Cover LetterAbout twenty "the" and "a' were deleted or added (not indicated).About fifteen commas were added (not indicated).Every "pH's" was converted to "pHs".Single form was changed to plural form and vice versa for some points.Other alterations are as follows. P2. Line 3: "has not been known" was change to "has not been hitherto understood". P2. Line 16: "solved" was deleted.P2. Line 17: "that" which had been deleted in the original manuscript was added.P2. Line 23 and others: "high alkaline pH's" was changed to "highly alkaline pHs". P3. Line 3: "till" was changed to "until".P3. Results and discussion, Lines 7 and 11 The order of words were changed from "slightly shifted" to "shifted slightly" and "in only" to "only in".P3. Line 5 from bottom: "with the spin Hamiltonian parameters" was added after "s...

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Section: Resultsmentioning

confidence: 99%

The alkaline transition of blue copper proteins, Cucumis sativus plastocyanin and Pseudomonas aeruginosa azurin

Sakurai¹

2006

FEBS Letters

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“…The alkaline transition of MCO has not been studied in detail but we have recently reported that bilirubin oxidase shows a dramatic alkaline transition [96]. With increasing pH values higher than 7, the characteristic blue color faded reversibly and the intensity of the type I copper EPR signal also changed concomitantly with the absorption change.…”

Section: Properties Of Type I Copper In Multicopper Oxidasesmentioning

confidence: 98%

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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“…Insight from crystals structures combined with molecular modelling would be desirable, in order to elucidate the obvious differences among BODs in substrate affinities (Table 1). Of particular interest is a series of papers by Sakurai et al in which they have reported the biochemical characterizations and electrochemical activity of several bilirubin oxidase mutants from M. verrucaria (Kamitaka et al 2007a;Kataoka et al 2005a;Shimizu et al 1999aShimizu et al , b, 2003Zoppellaro et al 2004).…”

Section: Biochemical Characterizationmentioning

confidence: 99%

Features and applications of bilirubin oxidases

Mano

2012

Appl Microbiol Biotechnol

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Discovered in 1981 by Tanaka and Murao (Agric Biol Chem 45:2383-2384, 1981), bilirubin oxidase (BOD) is a sub-group of multicopper oxidases (MCOs) also utilizing four Cu(+/2+) ions. It catalyzes the oxidation of bilirubin to biliverdin, hence the classification of bilirubin oxidase, and has been primarily used in the determination of bilirubin in serum and thereby in the diagnostic of jaundice. Unlike laccases, the most studied MCOs, BODs display a high activity and stability at neutral pH, a high tolerance towards chloride anions and other chelators, and for some species, a high thermal tolerance. Therefore, BODs could potentially be an alternative to laccase which are so far mainly restricted to applications in acid media. Because of growing interest in BODs for numerous applications under mild pH conditions, based on the number of patents and publications published in the last 5 years, here I will summarize the available data on the biochemical properties of BODs, their occurrence, and their possible biotechnological use in (1) the field of Healthcare for the elaboration of biofuel cells or bilirubin sensors or (2) the field of environmentally desirable applications such as depollution, decolorization of dyes, and pulp bleaching.

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The Reversible Change in the Redox State of Type I Cu inMyrothecium verrucariaBilirubin Oxidase Depending on pH

Cited by 13 publications

References 12 publications

The alkaline transition of blue copper proteins, Cucumis sativus plastocyanin and Pseudomonas aeruginosa azurin

The alkaline transition of blue copper proteins, Cucumis sativus plastocyanin and Pseudomonas aeruginosa azurin

Structure and function of type I copper in multicopper oxidases

Features and applications of bilirubin oxidases

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