T. Tosha

发表

Crystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus

Yuji Sugita, Andrei V. Pisliakov, Yoshitsugu Shiro, 2012, Nature Structural &Molecular Biology.

GATED PORES IN THE FERRITIN PROTEIN NANOCAGE.

Elizabeth C. Theil, T. Tosha, Xiaofeng S. Liu, 2008, Inorganica chimica acta.

Unique Peroxidase Reaction Mechanism in Prostaglandin Endoperoxide H Synthase-2

T. Uchida, K. Ishimori, I. Morishima, 2007, Journal of Biological Chemistry.

Impact of membrane protein-lipid interactions on formation of bilayer lipid membranes on SAM-modified gold electrode

I. Yagi, Masaru Kato, Y. Shiro, 2021 .

Ferritin Contains Less Iron (59Fe) in Cells When the Protein Pores Are Unfolded by Mutation*

Elizabeth C. Theil, T. Tosha, M. R. Hasan, 2008, Journal of Biological Chemistry.

Structural basis for promotion of duodenal iron absorption by enteric ferric reductase with ascorbate

H. Sugimoto, K. Hirata, T. Urano, 2018, Communications Biology.

Structural basis for promotion of duodenal iron absorption by enteric ferric reductase with ascorbate

H. Sugimoto, K. Hirata, T. Urano, 2018 .

Mononuclear copper(II)-hydroperoxo complex derived from reaction of copper(I) complex with dioxygen as a model of DbetaM and PHM.

H. Masuda, T. Ozawa, Y. Funahashi, 2006, Chemical communications.

Hijacking the Heme Acquisition System of Pseudomonas aeruginosa for the Delivery of Phthalocyanine as an Antimicrobial.

H. Sugimoto, O. Shoji, Yoshihito Watanabe, 2019, ACS chemical biology.

Effect of low temperature preservation and cell density on metabolic function in a bioartificial liver

H. Iwata, S. Fujita, H. Ryu, 2003 .

Structural Diversities of Active Site in Clinical Azole-bound Forms between Sterol 14α-Demethylases (CYP51s) from Human and Mycobacterium tuberculosis*

M. Waterman, N. Kagawa, K. Ishimori, 2005, Journal of Biological Chemistry.

Dimeric structures of quinol-dependent nitric oxide reductases (qNORs) revealed by cryo–electron microscopy

S. Antonyuk, S. Hasnain, Masaki Yamamoto, 2019, Science Advances.

The active form of quinol-dependent nitric oxide reductase from Neisseria meningitidis is a dimer

S. Antonyuk, S. Hasnain, S. Muench, 2020, IUCrJ.

Single crystal spectroscopy and multiple structures from one crystal (MSOX) define catalysis in copper nitrite reductases

S. Antonyuk, S. Hasnain, N. Scrutton, 2022, Proceedings of the National Academy of Sciences of the United States of America.

A nearly on-axis spectroscopic system for simultaneously measuring UV–visible absorption and X-ray diffraction in the SPring-8 structural genomics beamline

H. Sugimoto, M. Kubo, Masaki Yamamoto, 2016, Journal of synchrotron radiation.

Interaction between Substrate and Oxygen Ligand Responsible for Effective O–O Bond Cleavage in Bovine Cytochrome P450 Steroid 21-Hydroxylase Proved by Raman Spectroscopy*

M. Waterman, N. Kagawa, T. Tosha, 2008, Journal of Biological Chemistry.

Raman evidence for specific substrate-induced structural changes in the heme pocket of human cytochrome P450 aromatase during the three consecutive oxygen activation steps.

M. Waterman, N. Kagawa, T. Ohta, 2006, Biochemistry.

Regulation Mechanism of Cytochrome P450cam-Catalyzed Oxygenation Reaction upon Putidaredoxin Binding

K. Ishimori, I. Morishima, T. Tosha, 2005 .

An unprecedented dioxygen species revealed by serial femtosecond rotation crystallography in copper nitrite reductase

S. Antonyuk, S. Hasnain, K. Hirata, 2018, IUCrJ.

Transient intermediates from Mn(salen) with sterically hindered mesityl groups: interconversion between MnIV-phenolate and MnIII-phenoxyl radicals as an origin for unique reactivity.

H. Fujii, Y. Shiro, T. Kurahashi, 2008, Inorganic chemistry.

Timing of NO Binding and Protonation in the Catalytic Reaction of Bacterial Nitric Oxide Reductase as Established by Time-Resolved Spectroscopy

M. Kubo, Y. Shiro, Tetsunari Kimura, 2020 .

Heme controls the structural rearrangement of its sensor protein mediating the hemolytic bacterial survival

K. Tsumoto, H. Sugimoto, S. Nagatoishi, 2021, Communications Biology.

Synthesis and reactivity of (μ-η2:η2-peroxo)dicopper(II) complexes with dinucleating ligands : Hydroxylation of xylyl linker with a NIH shift

Takahiro Matsumoto, S. Fujinami, T. Tosha, 2007 .

Surface-Enhanced Infrared Absorption Spectroscopy of Bacterial Nitric Oxide Reductase under Electrochemical Control Using a Vibrational Probe of Carbon Monoxide.

I. Yagi, Masaru Kato, K. Nakata, 2018, The journal of physical chemistry letters.

Ferritins for Chemistry and for Life.

Elizabeth C. Theil, R. Behera, T. Tosha, 2013, Coordination chemistry reviews.

Serial Femtosecond Zero Dose Crystallography Captures a Water‐Free Distal Heme Site in a Dye‐Decolorising Peroxidase to Reveal a Catalytic Role for an Arginine in FeIV=O Formation

H. Sugimoto, A. Ebrahim, Michael T. Wilson, 2020, Angewandte Chemie.

Identification of an "end-on" nickel-superoxo adduct, [Ni(tmc)(O2)]+.

T. Brunold, W. Nam, T. Tosha, 2006, Journal of the American Chemical Society.

On the Relationship of Coral Allene Oxide Synthase to Catalase

T. Uchida, A. Brash, T. Kitagawa, 2006, Journal of Biological Chemistry.

Characterization of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus: enzymatic activity and active site structure.

Y. Sako, Y. Shiro, T. Tosha, 2014, Biochimica et biophysica acta.

Molecular structure and function of bacterial nitric oxide reductase.

H. Sugimoto, T. Hino, Y. Shiro, 2012, Biochimica et biophysica acta.

Characterization of the quinol-dependent nitric oxide reductase from the pathogen Neisseria meningitidis, an electrogenic enzyme

S. Antonyuk, S. Hasnain, K. Muramoto, 2018, Scientific Reports.

Proton transfer in the quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus during reduction of oxygen.

J. Reimann, Y. Shiro, T. Tosha, 2012, Biochimica et biophysica acta.

Short-lived intermediate in N2O generation by P450 NO reductase captured by time-resolved IR spectroscopy and XFEL crystallography

Daichi Yamada, H. Sugimoto, K. Hirata, 2021, Proceedings of the National Academy of Sciences.

Pseudomonas aeruginosa overexpression system of nitric oxide reductase for in vivo and in vitro mutational analyses.

H. Arai, H. Sawai, Y. Shiro, 2018, Biochimica et biophysica acta. Bioenergetics.

Structural basis for heme detoxification by an ATP-binding cassette–type efflux pump in gram-positive pathogenic bacteria

M. Shirouzu, T. Hisano, Y. Shiro, 2022, Proceedings of the National Academy of Sciences of the United States of America.

Regioselective arene hydroxylation mediated by a (mu-peroxo)diiron(III) complex: a functional model for toluene monooxygenase.

Kenji Takahashi, S. Fujinami, T. Tosha, 2007, Journal of the American Chemical Society.

Moving Iron through Ferritin Protein Nanocages Depends on Residues throughout Each Four α-Helix Bundle Subunit*

Elizabeth C. Theil, T. Tosha, S. Haldar, 2011, The Journal of Biological Chemistry.

Synthesis, characterization, and reactivities of manganese(V)-oxo porphyrin complexes.

E. Solomon, S. George, T. Ohta, 2007, Journal of the American Chemical Society.

CD and MCD spectroscopic studies of the two Dps miniferritin proteins from Bacillus anthracis: role of O2 and H2O2 substrates in reactivity of the diiron catalytic centers.

Jennifer K. Schwartz, Elizabeth C. Theil, E. Solomon, 2010, Biochemistry.

Roles of the proximal hydrogen bonding network in cytochrome P450cam-catalyzed oxygenation.

Satoshi Takahashi, K. Ishimori, H. Hori, 2002, Journal of the American Chemical Society.

Identifying antibiotics based on structural differences in the conserved allostery from mitochondrial heme-copper oxidases

K. Shimuta, M. Ohnishi, K. Shinzawa-Itoh, 2022, Nature communications.

Structure and dioxygen-reactivity of copper(I) complexes supported by bis(6-methylpyridin-2-ylmethyl)amine tridentate ligands.

S. Itoh, S. Fujinami, T. Tosha, 2005, Dalton transactions.

Solving Biology's Iron Chemistry Problem with Ferritin Protein Nanocages.

Elizabeth C. Theil, R. Behera, T. Tosha, 2016, Accounts of chemical research.

Fe2+ substrate transport through ferritin protein cage ion channels influences enzyme activity and biomineralization

Elizabeth C. Theil, C. Goulding, R. Behera, 2015, JBIC Journal of Biological Inorganic Chemistry.

The ferritin Fe2 site at the diiron catalytic center controls the reaction with O2 in the rapid mineralization pathway

Elizabeth C. Theil, T. Tosha, M. R. Hasan, 2008, Proceedings of the National Academy of Sciences.

Spectroscopic definition of the ferroxidase site in M ferritin: comparison of binuclear substrate vs cofactor active sites.

Jennifer K. Schwartz, Elizabeth C. Theil, E. Solomon, 2008, Journal of the American Chemical Society.

A mononuclear alkylperoxocopper(II) complex as a reaction intermediate in the oxidation of the methyl group of the supporting ligand.

Takahiro Matsumoto, S. Fujinami, Jaeheung Cho, 2006, Angewandte Chemie.

Moving metal ions through ferritin-protein nanocages from three-fold pores to catalytic sites.

Elizabeth C. Theil, H. Ng, T. Tosha, 2010, Journal of the American Chemical Society.

Formation of a Bridged Butterfly-Type μ-η2:η2-Peroxo Dicopper Core Structure with a Carboxylate Group

S. Hirota, H. Masuda, T. Ozawa, 2008 .

Intramolecular arene hydroxylation versus intermolecular olefin epoxidation by (mu-eta2:eta2-peroxo)dicopper(II) complex supported by dinucleating ligand.

Takahiro Matsumoto, S. Itoh, S. Fujinami, 2006, Journal of the American Chemical Society.

Spectroscopic Studies of Single and Double Variants of M Ferritin: Lack of Conversion of a Biferrous Substrate Site into a Cofactor Site for O2 Activation

Jennifer K. Schwartz, Elizabeth C. Theil, R. Behera, 2014, Biochemistry.

An unprecedented insight into the catalytic mechanism of copper nitrite reductase from atomic-resolution and damage-free structures

S. Antonyuk, S. Hasnain, K. Hirata, 2021, Science Advances.

Oxidation reactivity of bis(mu-oxo) dinickel(III) complexes: arene hydroxylation of the supporting ligand.

M. Kubo, Takahiro Matsumoto, T. Kitagawa, 2009, Angewandte Chemie.

17O NMR study of oxo metalloporphyrin complexes: correlation with electronic structure of M=O moiety.

H. Fujii, T. Yoshimura, T. Kurahashi, 2006, Journal of inorganic biochemistry.

Oxidation Reactivity of a Structurally and Spectroscopically Well-defined Mononuclear Peroxocarbonato–Iron(III) Complex

Y. Sakata, T. Ogura, Shigehisa Akine, 2015 .

Oxidizing intermediates from the sterically hindered iron salen complexes related to the oxygen activation by nonheme iron enzymes.

Yoshio Kobayashi, H. Fujii, T. Kurahashi, 2005, Inorganic chemistry.

Ferritin ion channel disorder inhibits Fe(II)/O2 reactivity at distant sites.

Elizabeth C. Theil, R. Behera, T. Tosha, 2012, Inorganic Chemistry.

Ferritin Protein Nanocage Ion Channels

Elizabeth C. Theil, H. Ng, R. Behera, 2012, The Journal of Biological Chemistry.

Capturing an initial intermediate during the P450nor enzymatic reaction using time-resolved XFEL crystallography and caged-substrate

Kunio Hirata, Makina Yabashi, Go Ueno, 2017, Nature Communications.

Structural basis for promotion of duodenal iron absorption by enteric ferric reductase with ascorbate

H. Sugimoto, K. Hirata, T. Urano, 2018, Communications Biology.

Dynamics of nitric oxide controlled by protein complex in bacterial system

Y. Sugita, H. Sugimoto, Takaharu Mori, 2017, Proceedings of the National Academy of Sciences.

Structures of reduced and ligand‐bound nitric oxide reductase provide insights into functional differences in respiratory enzymes

H. Sugimoto, Y. Sako, T. Hino, 2014, Proteins.

L358P Mutation on Cytochrome P450cam Simulates Structural Changes upon Putidaredoxin Binding

K. Ishimori, I. Morishima, T. Tosha, 2004, Journal of Biological Chemistry.

Time-resolved studies of metalloproteins using X-ray free electron laser radiation at SACLA.

H. Sugimoto, Jian-Ren Shen, T. Tosha, 2020, Biochimica et biophysica acta. General subjects.

Capturing an initial intermediate during the P450nor enzymatic reaction using time-resolved XFEL crystallography and caged-substrate

O. Nureki, K. Tono, M. Yabashi, 2017, Nature Communications.

NMR Study on the Structural Changes of Cytochrome P450cam upon the Complex Formation with Putidaredoxin

Satoshi Takahashi, K. Ishimori, I. Morishima, 2003, Journal of Biological Chemistry.

Serial Femtosecond Crystallography Reveals the Role of Water in the One- or Two-Electron Redox Chemistry of Compound I in the Catalytic Cycle of the B-Type Dye-Decolorizing Peroxidase DtpB

H. Sugimoto, Michael T. Wilson, J. Worrall, 2022, ACS catalysis.

XFEL Crystal Structures of Peroxidase Compound II

Samuel L. Freeman, K. Tono, H. Sugimoto, 2021, Angewandte Chemie.

Mechanism of substrate inhibition in cytochrome-c dependent NO reductases from denitrifying bacteria (cNORs).

S. D. de Visser, P. Hagedoorn, H. Matsumura, 2022, Journal of inorganic biochemistry.

Identification of a novel zinc-binding protein, C1orf123, as an interactor with a heavy metal-associated domain

S. Akiyama, Y. Furukawa, Y. Shiro, 2018, PloS one.

Efficient depolymerization of polyethylene terephthalate (PET) and polyethylene furanoate by engineered PET hydrolase Cut190

Yoshitomo Furushima, N. Muraki, M. Yamashita, 2022, AMB Express.

Synthesis and reactivity of a (mu-1,1-hydroperoxo)(mu-hydroxo)dicopper(II) complex: ligand hydroxylation by a bridging hydroperoxo ligand.

H. Hayashi, Takahiro Matsumoto, S. Fujinami, 2005, Journal of the American Chemical Society.

Structural and functional characterization of "laboratory evolved" cytochrome P450cam mutants showing enhanced naphthalene oxygenation activity.

Satoshi Takahashi, K. Ishimori, K. Matsuura, 2004, Biochemical and biophysical research communications.

Sequential reaction intermediates in aliphatic C-H bond functionalization initiated by a bis(mu-oxo)dinickel(III) complex.

T. Uruga, T. Kawai, A. Suzuki, 2006, Inorganic chemistry.

Nonheme iron(II) complexes of macrocyclic ligands in the generation of oxoiron(IV) complexes and the catalytic epoxidation of olefins.

Yumi Suh, Jinheung Kim, W. Nam, 2006, Journal of inorganic biochemistry.

Characterization of the quinol-dependent nitric oxide reductase from the pathogen Neisseria meningitidis, an electrogenic enzyme

S. Antonyuk, S. Hasnain, K. Muramoto, 2018, Scientific Reports.

Serial Femtosecond Crystallography Reveals that Photoactivation in a Fluorescent Protein Proceeds via the Hula Twist Mechanism

S. Boxer, K. Tono, S. Iwata, 2023, Journal of the American Chemical Society.

A redox switch allows binding of Fe(II) and Fe(III) ions in the cyanobacterial iron binding protein FutA from Prochlorococcus

G. Murshudov, I. Tews, J. Worrall, 2023, bioRxiv.

Trapping of a Mononitrosyl Nonheme Intermediate of Nitric Oxide Reductase by Cryo-Photolysis of Caged Nitric Oxide.

M. Kubo, Y. Shiro, Tetsunari Kimura, 2023, The journal of physical chemistry. B.

Catalytic Oxidation of Methane by Wild-Type Cytochrome P450BM3 with Chemically Evolved Decoy Molecules

H. Sugimoto, Shinya Ariyasu, O. Shoji, 2023, ACS Catalysis.

Crystal structures of nitric oxide reductases provide key insights into functional conversion of respiratory enzymes

Y. Shiro, T. Tosha, 2013, IUBMB life.

Human duodenal cytochrome b (Dcytb) in zinc ion and ascorbate bound form

K. Hirata, T. Urano, A. Mauk, 2018 .

Structural basis for binding and transfer of heme in bacterial heme‐acquisition systems

K. Tsumoto, H. Sugimoto, Y. Naoe, 2017, Proteins.

Transmission electron microscopic study of hepatocytes in bioartificial liver.

Y. Ikada, H. Iwata, S. Satoh, 2000, Tissue engineering.

Spectroscopic definition of the ferroxidase site in M ferritin: comparison of binuclear substrate vs cofactor active sites.

Jennifer K. Schwartz, Elizabeth C. Theil, E. Solomon, 2008, Journal of the American Chemical Society.

Moving metal ions through ferritin-protein nanocages from three-fold pores to catalytic sites.

Elizabeth C. Theil, H. Ng, T. Tosha, 2010, Journal of the American Chemical Society.

Crystal structure of quinol-dependent nitric oxide reductase from Geobacillus stearothermophilus

Andrei V. Pisliakov, Y. Sugita, H. Sugimoto, 2012, Nature Structural &Molecular Biology.

CD and MCD spectroscopic studies of the two Dps miniferritin proteins from Bacillus anthracis: role of O2 and H2O2 substrates in reactivity of the diiron catalytic centers.

Jennifer K. Schwartz, Elizabeth C. Theil, E. Solomon, 2010, Biochemistry.

Fe2+ substrate transport through ferritin protein cage ion channels influences enzyme activity and biomineralization

Elizabeth C. Theil, C. Goulding, R. Behera, 2015, JBIC Journal of Biological Inorganic Chemistry.

Oxygen-evolving photosystem II structures during S1–S2–S3 transitions

T. Hatsui, Y. Joti, M. Yabashi, 2024, Nature.

Time-resolved serial crystallography to track the dynamics of carbon monoxide in the active site of cytochrome c oxidase

R. Neutze, H. Naitow, K. Tono, 2023, Science advances.

Structures of reduced and ligand‐bound nitric oxide reductase provide insights into functional differences in respiratory enzymes

H. Sugimoto, Y. Sako, T. Hino, 2014, Proteins.

A redox switch allows binding of Fe(II) and Fe(III) ions in the cyanobacterial iron-binding protein FutA from Prochlorococcus

G. Murshudov, J. Worrall, G. Evans, 2023, bioRxiv.