金沢大学理工学研究域物質化学系生物化学研究室

Study on Dioxygen Reduction by Mutational Modifications of the Hydrogen Bond Network Leading from Bulk Water to the Trinuclear Copper Center in Bilirubin Oxidase;
H. Morishita, D. Kurita, K. Kataoka, and T. Sakurai,
Biochem. Biophys. Res. Commun., 450, 767-772 (2014)

New Insights into the Catalytic Active-Site Structure of Multicopper Oxidases;
H. Komori, R. Sugiyama, K. Kataoka, K. Miyazaki, Y. Higuchi and T. Sakurai,
Acta Cryst. D70, 772-779 (2014).

Crystal Structure of the CueO Mutants at Glu506, the Key Amino Acid Located in the Proton Transfer Pathway for Dioxygen Reduction;
H. Komori, T. Kajikawa, K. Kataoka, Y. Higuchi, and T. Sakurai,
Biochem. Biophys. Res. Commun., 438, 686-690 (2013)

Role of the Hydrogen Bond Connecting the Ligands for Substrate and Type I Copper in the Cuprous Oxidase, CueO;
K. Kataoka and T. Sakurai,
Chem. Lett. 42, 1102-1104 (2013)

Modifications of Laccase Activities of Copper Efflux Oxidase, CueO by Synergistic Mutations in the First and Second Coordination Spheres of the Type I Copper Center;
K. Kataoka, H. Kogi, S. Tsujimura, and T. Sakurai,
Biochem. Biophys. Res. Commun., 431, 393-397 (2013)

Electrochemical Characterization of a Unique "Neutral" Laccase from Flammulina velutipes;
K. Saito, S. Kurose, Y. Tsujino, T. Osakai, K. Kataoka, T. Sakurai, and E. Tamiya,
J. Biosci. Bioeng., 115, 159-167 (2013)

Modifications on the Hydrogen Bond Network by Mutations of Escherichia coli Copper Efflux Oxidase Affect the Process of Proton Transfer to Dioxygen Leading to Alterations of Enzymatic Activities;
T. Kajikawa, K. Kataoka, and T. Sakurai,
Biochem. Biophys. Res. Commun., 422, 152-156 (2012)

An O-Centered Structure of the Trinuclear Copper Center in the Cys500Ser/Glu506Gln Mutant of CueO and Structural Changes in Low to High X-Ray Dose Conditions;
H. Komori, R. Sugiyama, K. Kataoka, Y. Higuchi, and T. Sakurai,
Angewandte Chemie, 51, 1861-1864 (2012)

Multicopper Proteins, in Copper-Oxygen Chemistry (Eds by K.D. Karlin and S. Itoh), John Wiley &Sons, Inc., New Jersey, pp. 131-168 (2011),
T. Sakurai and K. Kataoka

Enhancement of Laccase Activity through the Construction and Breakdown of a Hydrogen Bond at the Type I Copper Center in Escherichia coli CueO and the Deletion Mutant Δα5-7 CueO;
K. Kataoka, S. Hirota, Y. Maeda, H. Kogi, N. Shinohara, M. Sekimoto, and T. Sakurai,
Biochemistry, 50, 558-565 (2011)

ATR–FTIR Study of the Protonation States of the Glu Residue in the Multicopper Oxidases, CueO and Bilirubin Oxidase;
M. Iwaki, K. Kataoka, T. Kajino, R. Sugiyama, H. Morishita, and T. Sakurai,
FEBS Lett., 584, 4027-4031 (2010)

Asymmetric Dimeric Structure of Ferredoxin-NAD(P)+ Oxidoreductase from the Green Sulfur Bacterium Chlorobacterium tepidum: Implications for Binding Ferredoxin and NADP+;
N. Muraki, D. Seo, T. SHiba, T. Sakurai, and G. Kurisu,
J. Mol. Biol., 401, 403-414 (2010)

Crystallization and Preliminary X-ray Studies of Ferredoxin-NADP+ Oxidoreductase Encoded by Bacillus subtilis yumC;
H. Komori, D. Seo, T. Sakurai, and Y. Higuchi,
Acta Cryst., F66, 301-303 (2010)

Four-Electron Reduction of Dioxygen by a Multicopper Oxidase, CueO, and Roles of Asp112 and Glu506 Located Adjacent to the Trinuclear Copper Center;
K. Kataoka, R. Sugiyama, S. Hirota, M. Inoue, K. Urata, Y. Minagawa, D. Seo, and T. Sakurai,
J. Biol. Chem., 284, 14405-14413 (2009)

Modification of Spectroscopic Properties and Catalytic Activity of Escherichia coli CueO by Mutations of Methionine 510, the Axial Ligand to the Type I Cu;
S. Kurose, K. Kataoka, N. Shinohara, Y. Miura, M. Tsutsumi, S. Tsujimura, K. Kano, and T. Sakurai,
Bull. Chem. Soc. Jpn., 82, 504-508 (2009)

Studies of Interaction of Homo-Dimeric Ferredoxin-NAD(P)+ Oxidoreductases of Bacillus subtiis and Rhodopseudomonas palustris, That Are Closely Related to Thioredoxin Reductase in Amino Acid Sequence, with Ferredoxins and Pyridine Nucleotide Coenzymes;
D. Seo, S. Okabe, M. Yanase, K. Kataoka, and T. Sakurai,
Biochim. Biophys. Acta, 1794, 594-601(2009)

Direct Electrochemistry of CueO and Its Mutants at Residues to and near Type I Cu for Oxygen-Reducing Biocathode;
Y. Miura, S. Tsujimura, S. Kurose, Y. Kamitaka, K. Kataoka, T. Sakurai, and K. Kano,
Fuel Cells, 9, 70-78 (2009)

Measurement of Electric Field Gradient at 117In on the Cu-site in Mavicyanin by Perturbed Angular Correlation of γ-rays;
A. Yokoyama, T. Hashimoto, K. Ihara, H. Kikunaga, N. Kinoshita, I. Yamazaki, K. Kataoka, M. Yanase, M. Takata, Y. Murakami, K. Takamiya, M. Tanigaki, and Y. Ohkubo,
Hyperfine Interactions, 181, 69-73 (2008)

Compensatory Binding of an Asparagine Residue to the Coordination-Unsaturated Type I Cu Center in Bilirubin Oxidase Mutants;
K. Kataoka, K. Tsukamoto, R. Kitagawa, T. Ito, and T. Sakurai,
Biochem. Biophys. Res. Commun., 371, 416-419 (2008)

Crystallization and Preliminary X-ray Studies of Ferredoxin-NAD(P)+ Reductase from Chlorobium tepidum;
N. Muraki, D. Seo, T. Shiba, T. Sakurai, and G. Kurisu,
Acta Cryst., F64, 186-189 (2008)

A Novel Zinc-Dependent D-Serine Dehydratase from Saccharomyces cerevisiae;
T. Ito, H. Hemmi, K. Kataoka, Y. Mukai, and T. Yoshimura,
Biochem J., 409, 399-406 (2008)

新たな展開を見せる漆の酵素　—マルチ銅オキシダーゼ;
櫻井　武, 化学と教育, 56, 74-75 (2008)

Structure and Function of Type I Copper in Multicopper Oxidases:
T. Sakurai, and K. Kataoka,
Cell. Mol. Life Sci., 64, 2642-2656 (2007)

Basic and Applied Features of Multicopper Oxidases, CueO, Bilirubin Oxidase, and Laccase:
T. Sakurai, and K. Kataoka,
Chem. Rec., 7, 220-229 (2007)

Structure and Function of the Engineered Multicopper Oxidase, CueO from Escherichia coli - Deletion of the Methionine-Rich Helical Region Covering the Substrate Binding Site -;
K. Kataoka, H. Komori, Y. Ueki, Y. Konno, Y. Kamitaka, S. Kurose, S. Tsujimura, Y. Higuchi, K. Kano, D. Seo, and T. Sakurai,
J. Mol. Biol., 373, 141-152 (2007)

Structure and Function of a Hexameric Copper-Containing Nitrite Reductase:
N. Nojiri, Y. Xie, T. Inoue, T. Yamamoto, H. Matsumura, K. Kataoka, Deligeer, K. Yamaguchi, Y. Kai, and S. Suzuki,
Proc. Natl. Acad. Sci. U.S.A., 104, 4315-4320 (2007)

Probing Electron Transfer Reactions between Two Azurins from Alcaligenes xylosoxidans GIFU 1051 with Optically Active Ru Complexes as Molecular Recognition Probes: Importance of the 43rd Residue:
T. Kato, H. Kumita, I, Takahashi, A. Murakami, K. Yoshimoto, Y. Ikeue, K. Kataoka, S. Suzuki, T. Sakurai, T. Ozawa, K. Jitsukawa, and H. Masuda,
Inorg. Chim. Acta, 360, 1555-1567 (2007)

Effect of Axial Ligand Mutation of the Type I Copper Site in Bilirubin Oxidase on Direct Electron Transfer-Type Bioelectrocatalytic Reduction of Dioxigen:
Y. Kamitaka, S. Tsujimura, K. Kataoka, T. Sakurai, T. Ikeda, and K. Kano,
Electroanal. Chem., 601, 119-124 (2007)

Promotion of Laccase Activities of Escherichia coli Cuprous Oxidase, CueO by Deleting the Segment Covering the Substrate Binding Site:
S. Kurose, K. Kataoka, K. Otsuka, Y. Tsujino, and T. Sakurai,
Chem. Lett., 36, 232-233 (2007)

Bioelectrocatalytic Reduction of O2 Catalyzed by CueO from Escherichia coli Adsorbed on a Highly Oriented Pyrolytic Graphite Electrode:
Y. Miura, S. Tsujimura, Y. Kamitaka, S. Kurose, K. Kataoka, T. Sakurai, and K. Kano,
Chem. Lett., 36, 132-133 (2007)

バイオ電気化学の実際　—バイオセンサ・バイオ電池の実用展開—
櫻井武, pp.92-100 (マルチ銅オキシダーゼ), 池田篤治編, シーエムシー出版, (2007)

Tandem and Single Genes of Three Membrane-Bound Nitrate Transporters in the nar Gene Cluster of the Moderately Halophilic Denitrifier, Halomonas halodenitrificans:
N. Sakurai, A. Asada, M. Mano, K. Kataoka, and T. Sakurai,
DNA Sequence, 17, 363-369 (2006)

Enzymatic and Spectroscopic Studies on the Activation or Inhibition Effects by Substituted Phenolic Compounds in the Oxidation of Aryldiamines and Catechols Catalyzed by Rhus vernicifera Laccase;
L. Casella, M. Gulloti, E. Monzani, L. Santagostini, G. Zoppellaro and T. Sakurai,
J. Inorganic Biochem., 100, 2127-2139 (2006)

Mutation at Asp112 Adjacent to the Trinuclear Cu Center in CueO as the Proton Donor in the Four-Electron Reduction of Dioxygen:
Y. Ueki, M. Inoue, S. Kurose, K. Kataoka, and T. Sakurai,
FEBS Lett., 580, 4069-4072 (2006)

銅のホメオスタシスに関与するマルチ銅オキシダーゼCueOの構造と機能;
櫻井武，片岡邦重
Biomed. Res. Trace Elements, 17, 308-315 (2006)

The Alkaline Transition of Blue Copper Proteins, Cucumis sativus Plastocyanin and Pseudomonas aeruginosa Azurin;
T. Sakurai,
FEBS Lett., 580, 1729-1732 (2006)

生命元素辞典
櫻井武, pp. 224-226 (3.5.1), pp. 379-382 (4.2.1), pp. 382-386 (4.2.2), 櫻井弘編, オーム社, (2006)

Characterization and Potential Application of Purified Aldehyde Oxidase from Pseudomonas stutzeli IFO 12695;
H. Uchida, T. Fukuda, Y. Satoh, Y. Okamura, A. Toriyama, A. Yamashita, K. Aisaka, T. Sakurai, Y. Nagaosa and T. Uwajima,
Appl. Microbiol. Biotechnol., 68, 53-56 (2005)

Solvent Effects on Electronic Structure of Active Site of Azurin by Polarizable Continuum Model;
K. Sugimori, T. Shiku, A. Sugiyama, H. Nagao, T. Sakurai and K. Nishikawa,
Polyhedron, 24, 2671-2675 (2005)

Molecular Orbital Analysis of Active Site of Oxidized Azurin: Dependency of Electronic Properties on Molecular Structure;
T. Shiku, K. Sugimori, A. Sugiyama, H. Nagao, T. Sakurai and K. Nishikawa,
Polyhedron, 24, 2665-2670 (2005)

Diverse NO Reduction by Halomonas halodenitrificans Nitric Oxide Reductase:
T. Sakurai, S. Nakashima, K. Kataoka, D. Seo, and N. Sakurai,
Biochem. Biophys. Res. Commun., 333, 483-487 (2005).

Point Mutation at the Type I Cu Ligands, Cys457 and Met467, and at the Putative Proton Donor, Asp105, in Myrothecium verrucaria Bilirubin Oxidase and Reaction with Dioxygen:
K. Kataoka, R. Kitagawa, M. Inoue, D. Naruse, T. Sakurai, and H. Huang,
Biochemistry, 44, 7004-7012 (2005)

High-Level Expression of Myrothecium verrucaria Bilirubin Oxidase in Pichia pastoris, and Its Facile Purification and Characterization:
K. Kataoka, K. Tanaka, Y. Sakai, and T. Sakurai,
Protein Expr. Purif., 41, 77-83 (2005)

Structural Reorganization of Copper Binding Site Involving Thr15 of Mavicyanin from Cucurbita pepo medullosa (Zucchini) upon Reduction:
Y. Xie, T. Inoue, Y. Miyamoto, H. Matsumura, K. Kataoka, K. Yamaguchi, S. Suzuki, and Y. Kai,
J. Biochem., 137, 455-461 (2005)

マルチ銅オキシドレダクターゼの構造と機能:
片岡邦重
生化学, 77, pp. 148-153 (2005)

Structure-Based Engineering of Alcaligenes xylosoxidans Copper-Containing Nitrite Reductase Enhances Intermolecular Electron Transfer Reaction with Pseudoazurin:
K. Kataoka, K. Yamaguchi, M. Kobayashi, T. Mori, N. Bokui, and S. Suzuki,
J. Biol. Chem., 51, 53374-53378 (2004)

Crystallization and Preliminary X-ray Crystallographic Studies of Dissimilatory Nitrite Reductase Isolated from Hyphomicrobium denitrificans A3151:
Y. Xie, T. Inoue, N. Seike, H. Matsumura, K. Kanbayashi, Deligeer, K. Itoh, K. Kataoka, K. Yamaguchi, S. Suzuki, and Y. Kai,
Acta Cryst., D60, 2383-2386 (2004)

Characterization of Two Type 1 Cu Sites of Hyphomicrobium denitrificans Nitrite Reductase: A New Class of Copper-containing Nitrite Reductases:
K. Yamaguchi, K. Kataoka, M. Kobayashi, K. Itoh, A. Fukui, and S. Suzuki:
Biochemistry, 43, 14180-14188 (2004)

The Reversible Change in the Redox State of Type I Cu in Myrothecium verrucaria Bilirubin Oxidase Depending on pH:
G. Zappellaro, N. Sakurai, K. Kataoka, and T. Sakurai,
Biosci. Biotechnol. Biochem., 68, 1998-2000 (2004)