Unraveling the unfolding mechanism of pseudoazurin: Insights into stabilizing cupredoxin fold as a common domain of Cu-containing proteins
Takahide Yamaguchi; Attila Taborosi; Kiyokazu Tsugane; Kathleen Wood; Andrew E. Whitten; Seiji Mori; Takamitsu Kohzuma, Lead, Elsevier BV
Journal of Inorganic Biochemistry, Jul. 2025, [Reviewed]

〔Major achievements〕Systematic elucidation of the second coordination sphere effect on the structure and properties of a blue copper protein, pseudoazurin
Takahide Yamaguchi; Attila Taborosi; Chihiro Sakai; Kohei Akao; Seiji Mori; Takamitsu Kohzuma, Lead
https://doi.org/10.1016/j.jinorgbio.2023.112292, 15 May 2023, [Reviewed]

Syntheses, Characterizations, Crystal Structures, and Protonation Reactions of Dinitrogen Chromium Complexes Supported with Triamidoamine Ligands
Yoshiaki Kokubo; Kazuki Tsuzuki; Hikari Sugiura; Shunsuke Yomura; Yuko Wasada-Tsutsui; Tomohiro Ozawa; Sachiko Yanagisawa; Minoru Kubo; Tomoyuki Takeyama; Takahide Yamaguchi; Yuichi Shimazaki; Shinichi Kugimiya; Hideki Masuda; Yuji Kajita, American Chemical Society (ACS)
Inorganic Chemistry, 27 Mar. 2023, [Reviewed]

Effect of structural iron on nanoscroll formation via exfoliation of a high iron-content kaolin.
Balázs Zsirka; Katalin Győrfi; Takahide Yamaguchi; Attila Táborosi; Veronika Vágvölgyi; Clara Parameswary; Zoltán Homonnay; Ernő Kuzmann; Erzsébet Horváth & János Kristóf
Journal of Materials Research, 20 Oct. 2022, [Reviewed]

Open-Bundle Structure as the Unfolding Intermediate of Cytochrome c′ Revealed by Small Angle Neutron Scattering
Takahide Yamaguchi; Kouhei Akao; Alexandros Koutsioubas; Henrich Frielinghaus; Takamitsu Kohzuma, Lead
Biomolecules, 07 Jan. 2022, [Reviewed]

2.85 and 2.99 Å resolution structures of 110 kDa nitrite reductase determined by 200 kV cryogenic electron microscopy
Naruhiko Adachi; Takahide Yamaguchi; Toshio Moriya; Masato Kawasaki; Kotaro Koiwai; Akira Shinoda; Yusuke Yamada; Fumiaki Yumoto; Takamitsu Kohzuma; ToshiyaSenda, Lead, Elsevier BV
Journal of Structural Biology, 16 Jul. 2021, [Reviewed]

Unusual Protein Stability of the Met16Leu Pseudoazurin Variant
Takahide Yamaguchi; Miyu Akatsu; Attila Taborosi; Takamitsu Kohzuma, Lead
Chemistry Letters, Dec. 2020, [Reviewed]

Effect of Cavity Size of Mesoporous Silica on Type 1 Copper Site Geometry in Pseudoazurin
Akira Yamaguchi; Yurie Edanami; Takahide Yamaguchi; Yuuta Shibuya; Norihisa Fukaya; Takamitsu Kohzuma
Bulletin of the Chemical Society of Japan, May 2020, [Reviewed]

The Role for the Weak Interaction on the Stabilization of Copper-Containing Complex: DFT Investigation of Noncovalent Interactions in Ternary-Cu(II) (DA)(AA) Complexes (DA = Diamine and AA = Amino Acids) as a Model of Metalloprotein
Attila Taborosi; Takahide Yamaguchi; Akira Odani; Osamu Yamauchi; Takamitsu Kohzuma
Bulletin of the Chemical Society of Japan, Nov. 2019, [Reviewed]

Computational Modelling Study on the Pseudoazurin Type 1 Cu Site　　　　　　　　　　　　　　　
Attila Taborosi; Takahide Yamaguchi; Seiji Mori; Takamitsu Kohzuma
JPS Conference Proceedings, Proceedings of the 3rd International Symposium of Quantum Beam Science at Ibaraki University "Quantum Beam Science in Biology and Soft Materials (ISQBSS2018)", Mar. 2019, [Reviewed]

Solution structure determination of a copper-containing nitrite reductase of achromobacter cycloclastes by small angle neutron scattering
Takahide Yamaguchi; Kathleen Wood; Attila Taborosi; Kouhei Akao; Takamitsu Kohzuma, A copper-containing nitrite reductase (NiR) catalyzes NO2 1 reduction in denitrifying bacteria. The reaction mechanism was proposed based on the trimeric crystal structure. In this study, a small angle neutron scattering (SANS) experiment with NiR from Achromobacter cycloclastes (AcNiR) was performed, and the first solution structure was obtained. The obtained radius of gyration, the calculation of the scattering curve from the available pdb structure and ab initio modelling all indicate a trimeric structure of AcNiR in solution., Chemical Society of Japan
Chemistry Letters, 2018

Stabilization of protein structure through - interaction in the second coordination sphere of pseudoazurin
Takahide Yamaguchi; Yuko Nihei; Duncan E. K. Sutherland; Martin J. Stillman; Takamitsu Kohzuma, Noncovalent, weak interactions in the second coordination sphere of the copper active site of Pseudoazurin (PAz) from Achromobacter cycloclastes were examined using a series of Met16X variants. In this study, the differences in protein stability due to the changes in the nature of the 16th amino acid (Met, Phe, Val, Ile) were investigated by electrospray ionization mass spectrometry (ESI-MS) and far-UV circular dichroism (CD) as a result of acid denaturation. The percentage of native states (folded holo forms) of Met16Phe variants was estimated to be 75% at pH 2.9 although the wild-type (WT), Met16Val and Met16Ile PAz, became completely unfolded. The high stability under acidic conditions is correlated with the result of the active site being stabilized by the aromatic substitution of the Met16 residue. The - interaction in the second coordination sphere makes a significant contribution to the stability of active site and the protein matrix., WILEY
PROTEIN SCIENCE, Oct. 2017, [Reviewed]

The pH Dependent Protein Structure Transitions and Related Spin State Transition of Cytochrome c’ from Alcaligenes xylosoxidans NCIMB 11015
Akiko Takashina; Michael T. Tiedemann; Masaki Unno; Takahide Yamaguchi; Martin J. Stillman; Takamitsu Kohzuma, The unusual magnetic/spectroscopic properties of Cytochrome c' (Cyt c') have been discussed, especially concerning the possibility of a quantum mechanically mixed-spin configuration of heme Fe(III). Here, four unique-spin species were identified from the magnetic circular dichroism (MCD) spectra of Cyt c' from Alcaligenes xylosoxidans (AxCyt c'). The electrospray ionization mass spectrometric (ESI-MS) and circular dichroism (CD) spectroscopic data showed the overall conformation of AxCyt c' was unchanged, in complete contrast to the drastic changes in the heme MCD spectra over the range of pH 3.5 and 11.8. The pH dependency of ESI-MS, electronic absorption, MCD, and CD spectroscopic properties of AxCyt c' enabled us to reveal the undiscovered correlation between the protein-folding state and the electronic structure of the active site as a function of pH. The mechanism of alkaline spin-state transition through the rearrangement of the hydrogen-bonding linkage between Helix C and D is also proposed on the basis of atomic resolution crystal structure analyses (A. Takashina, M. Unno, T. Kohzuma, Chem. Lett. 2015, 44, 268)., CHEMICAL SOC JAPAN
Bulletin of the Chemical Society of Japan, Feb. 2017, [Reviewed]

Molecular Science in Biology(3),– Quantum Beam, Synchrotron Radiation and X-ray Absorption Spectroscopy –
Takahide Yamaguchi and Takamitsu Kohzuma,

The 70 years have been passed from the first observation of synchrotron radiation. Recently, synchrotron radiation light source has been developped by new type of accelerator, and modern syncrtron has been dedicated and utilized to analyze the strucutres and properties of many variety of materials involving biomolecules. The histrical features of synchrtron radiation are overlooked, and synchrotron based X-ray absorption spectroscopy and related computational chemistry of metallo-protein are also introduced in this issue.

, Society of Computer Chemistry, Japan
Journal of Computer Chemistry, Japan, Dec. 2016, [Reviewed]

X-ray crystallographic evidence for the simultaneous presence of axial and rhombic sites in cupredoxins: atomic resolution X-ray crystal structure analysis of pseudoazurin and DFT modelling
Takahide Yamaguchi; Kohei Akao; Akiko Takashina; Sayaka Asamura; Masaki Unno; Robert K. Szilagyi and Takamitsu Kohzuma, Lead, Crystal structure refinement of pseudoazurin from Achromobacter cycloclastes (AcPAz) was carried out at atomic (1.10 angstrom) resolution. The copper ion was localized in two positions at the metal binding site of AcPAz. The occupancies of the copper sites are consistent with the ratio of axial and rhombic signals from EPR spectra and the intensity ratios for blue (axial) and green (rhombic) copper sites from UV-VIS spectroscopy. Computational modelling using an approximately 6 angstrom protein environment around the Cu site for both the oxidized and reduced forms showed that a small scale inner sphere rearrangement can account for the co-existence of two different redox active sites for a mononuclear cupredoxin independently from the employed density functionals., ROYAL SOC CHEMISTRY
RSC Advances, Sep. 2016, [Reviewed]

The Allosteric Regulation of Axial/Rhombic Population in a “Type 1” Copper Site: Multi-Edge X-ray Absorption Spectroscopic and Density Functional Studies of Pseudoazurin
Takahide Yamaguchi; Junko Yano; Vittal K. Yachandra; Yuko Nihei; Hiromi Togashi; Robert K. Szilagyi; Takamitsu Kohzuma, Lead, The co-existence of "axial" and "rhombic" coordination environments has been demonstrated in a "Type 1" copper site of Pseudoazurin. This observation opens up previously not considered interpretations for the relationship between geometry and electronic structure of the four coordinate copper site. The Met16 variants of pseudoazurin were considered as model systems for investigating the effect of weak interactions from the second coordination sphere. The correlation between geometric and electronic structures of "Type 1" copper site was evaluated by the multi-edge (Cu K-edge and S K-edge) X-ray absorption spectroscopy (XAS) of Met16 variants of pseudoazurin. The co-existing axial and rhombic sites in pseudoazurin were characterized by Cu ligand distances, effective nuclear charge, and Cu S(Cys) covalency from XAS. The XAS results were correlated with DFT calculations for investigating the effect of protein environment from the inner-sphere and beyond around the Cu site. The combined experimental and theoretical results support the presence of a close correlation between outer sphere environment and inner sphere coordination environment. This is achieved in pseudoazurin by a previously undisclosed allosteric effect that involves a rearrangement of the protein tertiary structure., CHEMICAL SOC JAPAN
Bulletin of the Chemical Society of Japan, Dec. 2015, [Reviewed]

Influence of Ligand Flexibility on the Electronic Structure of Oxidized NiIII-Phenoxide Complexes
Minoru Kawai; Takahide Yamaguchi; Shigeyuki Masaoka; Fumito Tani; Takamitsu Kohzuma; Linus Chiang; Tim Storr; Kaoru Mieda; Takashi Ogura; Robert K. Szilagyi; and Yuichi Shimazaki, One-electron-oxidized Ni-III-phenoxide complexes with salen-type ligands, [Ni(salen)py(2)](2+) ([1(en)-py](2+)) and [Ni(1,2-salcn)py(2)](2+) ([1(cn)-py](2+)), with a five-membered chelate dinitrogen backbone and [Ni(salpn)py(2)](2+) ([2(pn)-py](2+)) with a six-membered chelate backbone, have been characterized with a combination of experimental and theoretical methods. The five-membered chelate complexes [1(en)-py](2+) and [1(cn)-py](2+) were assigned as Ni-III-phenoxyl radical species, while the six-membered chelate complex [2(pn)-py](2+) was concluded to be a Ni-II-bis(phenoxyl radical) species with metal-centered reduction in the course of the one-electron oxidation of the Ni-III-phenoxide complex [2(pn)-py](+). Thus, the oxidation state of the one-electron-oxidized Ni-III salen-type complexes depends on the chelate ring size of the dinitrogen backbone., AMER CHEMICAL SOC
Inorganic Chemistry, Oct. 2014, [Reviewed]

The type 1 copper site of pseudoazurin: Axial and rhombic
Peter Gast; Freek G.J. Broeren; Silvia Sottini; Risa Aoki; Akiko Takashina; Takahide Yamaguchi; Takamitsu Kohzuma; Edgar J.J. Groenen, We report on a high-frequency electron-paramagnetic-resonance study of the type 1 copper site of pseudoazurin. The spectra fully resolve the contribution of a nearly axial spectrum besides the rhombic spectrum, which unequivocally proves the existence of two conformations of the copper site. Pseudoazurins have been considered from Achromobacter cycloclastes including eight mutants and from Alcaligenes faecalis. The two conformations are virtually the same for all pseudoazurins, but the rhombic/axial population varies largely, between 91/9 and 33/67. These observations are discussed in relation to optical absorption spectra and X-ray diffraction structures. A similar observation for fern plastocyanin from Dryopteris crassirhizoma suggests that dual conformations of type 1 copper sites are more common. (C) 2014 Elsevier Inc. All rights reserved., ELSEVIER SCIENCE INC
Journal of Inorganic Biochemistry, Aug. 2014, [Reviewed]

金属タンパク質の構造・電子状態を制御する外圏の弱い相互作用　　　　　　　　　　　　　　　
高妻孝光; 山口峻英; 高階明子; 海野昌喜
茨城大学iFRC年報 平成26年度, Sep. 2015

X-ray crystallographic structure analyses and characterization of a blue copper protein, pseudoazurin, Met16Ile variant
Kana Gunji; Takahide Yamaguchi; Akiko Takashina; Masaki Unno; Takamitsu Kohzuma
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, Aug. 2014

Geometry and electronic structures of axial/rhombic site in pseudoazurin Met16 variants: XAS and DFT investigations
Takahide Yamaguchi; Junko Yano; Vittal K. Yachandra; Robert K. Szilagyi; Takamitsu Kohzuma
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, Aug. 2014

クライオ電子顕微鏡ハンドブック　　　　　　　　　　　　　　　
難波 啓一、加藤 貴之、牧野 文信 他, Contributor
株式会社エヌ・ティー・エス, Jan. 2023
9784860438043

ラッカーゼのアミノ酸修飾 Au(111)電極へのエナンチオ選択的 吸着と酸素還元活性　　　　　　　　　　　　　　　
加藤優; 岡紗雪; 大橋龍人; 松島永佳; 山口峻英; 菅井碧宙; 星野翔吾; 八木一三
日本表面真空学会東北・北海道支部 令和6年度学術講演会, Mar. 2025
20250310, 20250311

シュウドアズリンMet16Gly変異体の構造と性質　　　　　　　　　　　　　　　
菅井 碧宙; 山口 峻英; 高妻 孝光
第50回 生体分子科学討論会, 22 Jun. 2024
20240621, 20240622

亜硝酸還元酵素Met56Phe変異体の性質　　　　　　　　　　　　　　　
篠塚 花音; 稲葉 直人; 山口 峻英; 高妻 孝光
第50回 生体分子科学討論会, 22 Jun. 2024
20240621, 20240622

中性子準弾性散乱によるシュウドアズリンMet16変異体のナノ・ピコ秒ダイナミクス解析　　　　　　　　　　　　　　　
橋本 将太; 山口 峻英; Kathleen Wood; Alice Klapproth; 高妻 孝光
第50回 生体分子科学討論会, 22 Jun. 2024
20240621, 20240622

中性子小角散乱と MD 計算によるシュウドアズリン Met16 変 異体の変性過程の解析　　　　　　　　　　　　　　　
山口 峻英; Taborosi Attil; 津金 聖和; Wood Kathleen; Andrew Whitte; 森 聖治; 高妻 孝光
第50回 生体分子科学討論会, 21 Jun. 2024
20240621, 20240622

ブルー銅タンパク質シュウドアズリンMet16X変異体を用いたタンパク質内弱い相互作用の系統的研究　　　　　　　　　　　　　　　
高妻 孝光、山口 峻英、Taborosi Attila、森 聖治
日本薬学会第143年会, Mar. 2023
20230325, 20230328

Tuning of the Cu Site Properties and Protein Stability by the Noncovalent Interactions in Second Coordination Sphere of Pseudoazurin　　　　　　　　　　　　　　　
Takahide Yamaguchi; Attila Taborosi; Wood Kathleen; Whitten Andrew; Seiji Mori; Takamitsu Kohzuma
10th Asian Biological Inorganic Chemistry (AsBIC10), Nov. 2022
20221128, 20221203

Second Coordination Sphere Effects on the Stability and Unfolding of Pseudoazurin　　　　　　　　　　　　　　　
山口 峻英・Taborosi Attila・津金 聖和・Wood Kathleen・Whitten Andrew・高妻 孝光
錯体化学会第72回討論会, 27 Sep. 2022
20220926, 20220928

クライオ電子顕微鏡による亜硝酸還元酵素のパッキングフリー構造解析　　　　　　　　　　　　　　　
山口 峻英; 安達 成彦; 守屋 俊夫; 川崎 政夫; 小祝 孝太郎; 篠田 晃; 山田 悠介; 湯本 史明; 高妻 孝光; 千田 俊哉
第48回生体分子科学討論会, 30 Jun. 2022
20220630, 20220701

Small angle X-ray scattering of lactase and stellacyanin from Okukuji lacquer sap　　　　　　　　　　　　　　　
菅井碧宙、中山綾乃、山口峻英、高妻孝光
第３１回金属の関与する生体関連反応シンポジウム, 18 Jun. 2022
20220618, 20220619

Effect of Noncovalent Weak Interaction in Pseudoazurin Met16Glu variant　　　　　　　　　　　　　　　
第３１回金属の関与する生体関連反応シンポジウム, 18 Jun. 2022
20220618, 20220619

Rational Elucidation of the Structure and Function for the Weak Interaction in Protein through a Pseudoazuin Met16X Variants　　　　　　　　　　　　　　　
Takahide Yamaguchi; Attila Taborosi; Seiji Mori; Takamitsu Kohzuma
第２２回日本蛋白質科学会年会, 08 Jun. 2022
20220607, 20220609

還元型Cytochrome c'のX線結晶構造解析　　　　　　　　　　　　　　　
2021年度量子ビームサイエンスフェスタ, 09 Mar. 2022
20220307, 20220309

量子ビームによる絹の染色機構に関する研究　　　　　　　　　　　　　　　
2021年度量子ビームサイエンスフェスタ, 08 Mar. 2022
20220307, 20220309

Alcaligenes xylosoxidans由来のAzurin IIの結晶構造解析　　　　　　　　　　　　　　　
2021年度量子ビームサイエンスフェスタ, 08 Mar. 2022
20220307, 20220309

Structural Stability and X-ray Crystal Structure of Met16Glu Mutant　　　　　　　　　　　　　　　
2021年度量子ビームサイエンスフェスタ, 08 Mar. 2022
20220307, 20220309

SAXSによるウルシ由来ステラシアニンの構造解析　　　　　　　　　　　　　　　
2021年度量子ビームサイエンスフェスタ, 08 Mar. 2022
20220307, 20220309

SAXSによる奥久慈産漆由来ラッカーゼの溶液構造　　　　　　　　　　　　　　　
2021年度量子ビームサイエンスフェスタ, 08 Mar. 2022
20220307, 20220308

弱い相互作用によるシュウドアズリンの構造安定性と変性状態の変化　　　　　　　　　　　　　　　
津金 聖和; 山口 峻英; Attila Taborosi; Kathleen Wood; Andrew Whitten; 高妻 孝光
第30回金属の関与する生体関連反応シンポジウム, 18 Jun. 2021
20210618, 20210619

奥久慈漆由来ラッカーゼ、ステラシアニンの単離と性質　　　　　　　　　　　　　　　
菅井碧宙; 山口 峻英; 高妻 孝光
第30回金属の関与する生体関連反応シンポジウム, 18 Jun. 2021
20210618, 20210619

Alcaligenes xylosoxidans由来のAzurin I, Azurin IIの精製と結晶構造解析　　　　　　　　　　　　　　　
稲葉 直登; 山口 峻英; 高妻 孝光
第30回金属の関与する生体関連反応シンポジウム, 18 Jun. 2021
20210618, 20210619

シュウドアズリン Met16Phe 変異体の還元型 X 線結晶構造解析　　　　　　　　　　　　　　　
青山 雄亮; 山口 峻英; 高妻 孝光
第30回金属の関与する生体関連反応シンポジウム, 18 Jun. 2021
20210618, 20210619

還元型 Cytochrome c’の X 線結晶構造解析　　　　　　　　　　　　　　　
鶴野 湧哉; 山口 峻英; 高妻 孝光
第30回金属の関与する生体関連反応シンポジウム, 18 Jun. 2021
20210618, 20210619

Second Coordination Effects in Blue Copper Protein with Combined Experimental and Computational Chemistry　　　　　　　　　　　　　　　
Takahide Yamaguchi; Attila Taborosi; Seiji Mori; Takamitsu Kohzuma
The 24th International Annual Symposium on Computational Science and Engineering (ANSCSE24), 30 Apr. 2021, [Invited]
20210428, 20210430

Tuning of type 1 copper site and stability through the non-covalent weak interaction in second coordination sphere of blue copper protein　　　　　　　　　　　　　　　
Takahide Yamaguchi; Taborosi Attila; Takamitsu Kohzuma
The 5th International Symposium of Quantum Beam Science, 19 Nov. 2020, [Invited]
20201119, 20201121

SANSによるブルー銅タンパク質シュウドアズリンのpH構造転移の解明　　　　　　　　　　　　　　　
津金 聖和; 山口 峻英; Attila Taborosi; Kathleen Wood; Andrew Whitten; 高妻 孝光
錯体化学会 第70回討論会, 30 Sep. 2020
20200928, 20200930

QENS Studies on the Detection of Domain Dynamics of Pseudoazurin Met16Ile Variant　　　　　　　　　　　　　　　
Shota HASHIMOTO; Takahide YAMAGUCHI; Attila TABOROSI; Kathleen WOOD; Alice KLAPPROTH; Takamitsu KOHZUMA
錯体化学会 第70回討論会, 30 Sep. 2020
20200928, 20200930

Structure Determination of the Open-Bundle Unfolding Intermediate of Cytochrome c’ by Small Angle Neutron Scattering　　　　　　　　　　　　　　　
Takahide Yamaguchi
The 70th JSCC Conference,"New Era of Bioinorganic Chemistry Developed by the Quantum Beam and,High Performance Computational Science", 28 Sep. 2020, [Invited]
20200928, 20200930

シュウドアズリンMet16変異体のpH構造転移　　　　　　　　　　　　　　　
津金聖和; 山口峻英; Taborosi Attila; Kathleen Wood; Andrew Whitten; 高妻孝光
第３０回日本化学会関東支部茨城地区研究交流会, 20 Dec. 2019

シュウドアズリンMet16Leu変異体の構造安定性　　　　　　　　　　　　　　　
赤津美結; 山口峻英; 高妻孝光
第３０回日本化学会関東支部茨城地区研究交流会, 20 Dec. 2019

QENSによるシュウドアズリンの構造ダイナミクス測定　　　　　　　　　　　　　　　
橋本将太; 山口峻英; Taborosi Attila; Kathleen Wood; Alice Klapproth; 高妻孝光
第３０回日本化学会関東支部茨城地区研究交流会, 20 Dec. 2019

The Strong Weak Interaction in Blue Copper Protein　　　　　　　　　　　　　　　
高妻孝光; 山口峻英; Taborosi Attila
第３０回日本化学会関東支部茨城地区研究交流会, 20 Dec. 2019

Elucidation of the weak interactions at the second coordination sphere of protein molecule: Structural and energetic studies of S-π, π-π, and CH-π interactions in Met16X Pseudoazurin.　　　　　　　　　　　　　　　
Attila Taborosi; Takahide Yamaguchi; Chihiro Sakai; Kohei Akao; Seiji Mori; Takamitsu Kohzuma
4th International Symposium of Quantume Beam Science, Oct. 2019

Computational chemistry study on the effect of noncovalent interactions in ternary-Cu(II) complexes, and on the blue copper protein Pseudoazurin Cu(II) active site.　　　　　　　　　　　　　　　
Attila Taborosi; Takahide Yamaguchi; Seiji Mori; Takamitsu Kohzuma
IMS Supercomputer Workshop 2018, Jan. 2019

Solution Structure Analysis of Nitrite Reductase by Small Angle Neutron Scattering　　　　　　　　　　　　　　　
Takahide Yamaguchi; Kathleen Wood; Takamitsu Kohzuma
第28回金属の関与する生体関連反応シンポジウム, Jun. 2018

Met16Ali(Ali=Aliphatic amino acids)シュウドアズリン変異体における弱い相互作用の効果　　　　　　　　　　　　　　　
高妻孝光; 酒井千尋; 山口峻英
第28回金属の関与する生体関連反応シンポジウム, Jun. 2018

Solution Structure Analysis of Blue Copper Protein by Small Angle Neutron Scattering　　　　　　　　　　　　　　　
Takahide Yamaguchi; kathleen Wood; Takamitsu Kohzuma
3rd International Symposium of Quantum Beam Science at Ibaraki University, 31 May 2018

The Structure and Function of Weak Interaction in Blue Copper Protein　　　　　　　　　　　　　　　
Takamitsu Kohzuma; Chihiro Sakai; Takahide Yamaguchi
3rd International Symposium of Quantum Beam Science at Ibaraki University, 31 May 2018

Solution Structure of Nitrite Reductase from Achromobacter cycloclasetes by Small Angle Neutron Scattering Method　　　　　　　　　　　　　　　
3rd International Symposium of Quantum Beam Science at Ibaraki University, 31 May 2018

タンパク質中の電子移動反応における活性中心近傍の弱い相互作用の効果　　　　　　　　　　　　　　　
山口 峻英; 赤尾 康平; 高妻 孝光
日本化学会第９８春季年会, Mar. 2018

In silico examination of non-bonding interactions in proteins　　　　　　　　　　　　　　　
Attila Taborosi; Takahide Yamaguchi; Takehiro Sato; Seiji Mori; Takamitsu Kohzuma
日本化学会第９８春季年会, Mar. 2018

Structure and Properties of a Side-Loop Variant, Met16Gly Pseudoazurin　　　　　　　　　　　　　　　
6th International Symposium on Metallomics, Aug. 2017

Additivity of the Structure and Properties in Protein Molecule　　　　　　　　　　　　　　　
2016年度量子ビームサイエンスフェスタ, Mar. 2017

Re-Investigation of Blue Copper Protein: Allosteric Structural Regulation of Type 1 Cu Site　　　　　　　　　　　　　　　
Thai-Japan Symposium in Chemistry, 15 Nov. 2016, [Invited]

弱い相互作用によるブルー銅タンパク質活性中心のアロステリック制御　　　　　　　　　　　　　　　
錯体化学会第66回討論会, 10 Sep. 2016

2022 - Present, Protein Science Society of Japan

2016 - Present, 錯体化学会

日本化学会