Presented papers

2017

1.

HmuS from Yersinia pseudotuberculosis is a non-canonical heme-degrading enzyme to acquire iron from heme

Masato Onzuka, Yukari Sekine, Takeshi Uchida, Koichiro Ishimori, and Shin-ichi Ozaki

Biochimica et Biophysica Acta (BBA) 2017, in press

2.

The Iron Chaperone Protein CyaY from Vibrio cholerae is a Heme-Binding Protein

Takeshi Uchida, Noriyuki Kobayashi, Souichiro Muneta, and Koichiro Ishimori

Biochemistry 2017, 56, 2425

3.

Heme iron coordination structure of heme transport protein HutB from Vibrio cholerae

Takeshi Uchida,Takumi, Funamizu, Mariko Ogura, and Koichiro Ishimori

Bull. Chem. Soc. Jpn., 2017, in press

4.

Heme Proximal Hydrogen Bonding between His170 and Asp132 Plays an Essential Role in the Heme Degradation Reaction by HutZ from Vibrio cholerae

Uchida Takeshi, Dojun Nobuhiko, Sekine Yukari, Ishimori Koichiro

Biochemistry 2017, in press

5.

 

 

 

 

 

 

2016

1.

Energetic Mechanism of Cytochrome c – Cytochrome c Oxidase Electron Transfer Complex Formation under Turnover Conditions Revealed by Mutational Effects and Docking Simulation

Wataru Sato, Seiji Hitaoka, Kaoru Inoue, Mizue Imai, Tomohide Saio,Takeshi Uchida, Kyoko Shinzawa-Itoh, Shinya Yoshikawa,Kazunari Yoshizawa and Koichiro Ishimori

J. Biol. Chem.2016, 291, 15320

2.

Structural Characterization of Heme Environmental Mutants of CgHmuT that Shuttles Heme Molecules to Heme Transporters

Norifumi Muraki, Chihiro Kitatsuji, Mariko Ogura, Takeshi Uchida, Koichiro Ishimori, and Shigetoshi Aono

Int. J. Mol. Sci. 201617(6), 829 

3.

Redox-Dependent Dynamics in Heme-Bound Bacterial Iron Response Regulator (Irr) Protein

Kazuo Kobayashi, Megumi Nakagaki, Haruto Ishikawa, Kazuhiro Iwai, Mark R. O’Brian and Koichiro Ishimori

Biochemistry2016, 55(29), 4047

4.

Energetic basis on interactions between ferredoxin and ferredoxin NADP+ reductase at varying physiological conditions

Misaki Kinoshita, Ju Yaen Kim, Satoshi Kume, Yuxi Lin, K. Hun Mok, Yosky Kataoka, Koichiro Ishimori, Natalia Markova, Genji Kurisu, Toshiharu Hase, Young-Ho Lee

Biochem. Biophys. Res. Commun.2017, 428, 909

5.

Dual role of the active-center cysteine in human peroxiredoxin 1: Peroxidase activity and heme binding

Yuta Watanabe, Koichiro Ishimori, Takeshi Uchida

Biochem. Biophys. Res. Commun., 2017, 483, 930 

6.

Iron Chelators Inhibit the Heme-Degradation Reaction by HutZ from Vibrio cholerae

Nobuhiko Dojun,  Yukari Sekine,  Koichiro Ishimori and Takeshi Uchida

Dalton Trans.2017,46, 5147 

 

 

2015

1.

A dye-decolorizing peroxidase from Vibrio cholerae

T. Uchida, M. Sasaki, Y. Tanaka, K. Ishimori

Biochemistry2015, 54, 6610

2.

Investigation of the redox-dependent modulation of structure and dynamics in human cytochrome c

M. Imai, T. Saio, H. Kumeta, T. Uchida, F. Inagaki, K. Ishimori

Biochem. Biophys. Res. Commun.2016, 469, 978 

3.

Conformational disorder of the most immature Cu,Zn-superoxide dismutase leading to amyotrophic lateral sclerosis

Y. Furukawa, I. Anzai, S. Akiyama, M. Imai, F. J. C. Cruz, T. Saio, K. Nagasawa, T. Nomura, K. Ishimori

J. Biol. Chem.2016, 291, 4144.

DOI: 10.1074/jbc.M115.683763

4.

Protein oxidation mediated by heme-induced active site conversion specific for heme-regulated transcription factor, iron response regulator

C. Kitatsuji, K. Izumi, S. Nambu, M. Kurogochi, T. Uchida, S. Nishimura, K. Iwai, M. R. O’Brian, M. Ikeda-Saito, K. Ishimori

Sci. Rep.2016, 6:18703, 1

 

5.

Cytoplasmic heme-binding protein (HutX) from Vibrio cholerae is an intracellular heme transport protein for the heme-degrading enzyme, HutZ 

Yukari Sekine, Takehito Tanzawa, Yoshikazu Tanaka, Koichiro Ishimori, Takeshi Uchida

Biochemistry, 2016, 55(6), 884

DOI: 10.1021/acs.biochem.5b01273

 

6.

Amorphous aggregation of cytochrome c with inherently low amyloidogenicity is characterized by the metastability of supersaturation and the phase diagram

Yuxi Lin, József Kardos, Mizue Imai, Tatsuya Ikenoue, Misaki Kinoshita, Toshihiko Sugiki, Koichiro Ishimori,Yuji Goto, and Young-Ho Lee

Langmuir, 2016, 32(8), 2010

7.

Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistance

Yasuaki Kabe,Takanori Nakane,Ikko Koike,Tatsuya Yamamoto,Yuki Sugiura,Erisa Harada,Kenji Sugase,Tatsuro Shimamura,Mitsuyo Ohmura,Kazumi Muraoka,Ayumi Yamamoto,Takeshi Uchida,So Iwata,Yuki Yamaguchi,Elena Krayukhina,Masanori Noda,Hiroshi Handa,Koichiro Ishimori,Susumu Uchiyama,Takuya Kobayashi& Makoto Suematsu

Nature Communications, 2016, 7, 11030

 

 

2014

1.

Spectroscopic studies on HasA from Yersinia pseudotuberculosis
S. Ozaki, T. Sato, Y. Sekine, C. T. Migita, T. Uchida and K. Ishimori

J. Inorg. Biochem., Vol. 138, 31-38 (2014).

2.

Molecular Mechanism for Heme-Mediated Inhibition of 5-Aminolevulinic Acid Synthase 1

C. Kitatsuji, M. Ogura, T. Uchida, K. Ishimori and S. Aono

Bull. Chem. Soc. Jpn., Vol. 87, 997-­1004 (2014)

3.

Heme-binding properties of HupD functioning as a substrate-binding protein in a 
heme-uptake ABC-transporter system in Listeria monocytogenes

Y. Okamoto, H. Sawai, M. Ogura, T. Uchida, K. Ishimori, T. Hayashi and S. Aono

Bull. Chem. Soc. Jpn.,

4.

Unique Heme Environmental Structures in Heme-regulated Proteins Using 
Heme as the Signaling Molecule

K. Ishimori and Y. Watanabe

Chem. Lett., in press

 

2013

1.

Sequence and Temperature Dependence of the End-to-End Collision Dynamics of Single-Stranded DNA
T. Uzawa, T. Isoshima, Y. Ito, K. Ishimori, D. E. Makarov and K. W. Plaxco
Biophys. J., Vol. 104, 2485-2492 (2013).

 

2012

1.

Effects of the bHLH Domain on Axial Coordination of heme in the PAS-A Domain of Neuronal PAS Domain Protein 2 (NPAS2): Conversion from His119/Cys170 Coordination to His119/His171 Coordination
T. Uchida, I. Sagami, T. Shimizu, K. Ishimori, and T. Kitagawa
J. Inorg. Biochem., Vol. 108, 188-195 (2012).

2.

The Structural Investigation on Small Methane Clusters Described by Two Different Potentials
H. Takeuchi
Comput. Theor. Chem., Vol. 986, 48-56 (2012).

3.

Function of Heme Regulatory Motif in the Oxidative Modification for Transcriptional Regulation
T. Tatsukawa, T. Uchida, and K. Ishimori
Peptide Sci., Vol. 2011, 191-192 (2012).

4.

A Heme Degradation Enzyme, HutZ, from Vibrio cholerae
T. Uchida, Y. Sekine, T. Matsui, M. Ikeda-Saito, and K. Ishimori
Chem. Commun., Vol. 48, 6741-6743 (2012).

5.

Structural Features of Small Benzene Clusters (C6H6)n (n ≤ 30) As Investigated with the All-Atom OPLS Potential
H. Takeuchi
J. Phys. Chem. A, Vol. 116, 10172-10181 (2012).

6.

The Structural Investigation on Small Methane Clusters Described by Two Different Potentials
H. Takeuchi
Comput. Theor. Chem., Vol. 986, 48-56 (2012).

 

2011

1.

Probing Phenylalanine Environments in Oligomeric Structures with Pentafluorophenylalanine and Cyclohexylalanine
T. Nomura, R. Kamada, I. Ito, K. Sakamoto, Y. Chuman, K. Ishimori, Y. Shimohigashi, K. Sakaguchi
Biopolymer, Vol. 95, 410-419 (2011).

2.

A Theoretical Investigation on Optimal Structures of Ethane Clusters (C2H6)n with n ≤ 25 and Their Building-up Principle
H. Takeuchi
J. Comput. Chem., Vol. 32, 1345-1352 (2011).

3.

Unusual Heme Binding in the Bacterial Iron Response Regulator Protein (Irr): Spectral Characterization of Heme Binding to Heme Regulatory Motif
H. Ishikawa, M. Nakagaki, A. Bamba, T. Uchida, H. Hori, M. R. O’Brian, K. Iwai, and K. Ishimori
Biochemistry, Vol. 50, 1016-1022 (2011).

4.

NMR Basis for Interprotein Electron Transfer Gating between Cytochrome c – Cytochrome c Oxidase
K. Sakamoto, M. Kamiya, M. Imai, K. Shinzawa-Ito, T. Uchida, K. Kawano, S. Yoshikawa, and K. Ishimori
Proc. Natl. Acad. Sci. U.S.A., Vol. 108, 12271-12276 (2011).

5.

Identification and Functional and Spectral Characterizations of a Novel Globin-Coupled Histidine Kinase from Anaeromixobacter sp. Fw109-5
K. Kitanishi, K. Kobayashi, T. Uchida, K. Ishimori, J. Igarashi, and T. Shimizu
J. Biol. Chem., Vol. 286, 35522-35534 (2011).

6.

Theoretical Investigation on Structural Properties of Ethylene Clusters (C2H4)n (n ≤ 25)
H. Takeuchi
Comput.Theor. Chem., Vol. 970, 48-53 (2011).

 

2010

1.

Molecular Oxygen Regulates the Enzymatic Activity of a Heme-containing Diguanylate Cyclase (HemDGC) for the Synthesis of Cyclic Di-GMP
H. Sawai, S. Yoshioka, T. Uchida, M. Hyodo, Y. Hayakawa, K. Ishimori, and S. Aono
Biochimica et Biophysica Acta, Vol. 1804, No. 1, 166-172 (2010).

2.

Global Minimum Geometries of Acetylene Clusters (HCCH)n with n ≤ 55 Obtained by a Heuristic Method Combined with Geometrical Perturbations
H. Takeuchi
J. Comput. Chem., Vol. 31, No. 8, 1699-1706 (2010).

3.

Redox-controlled Backbone Dynamics of Human Cytochrome c Revealed by 15N NMR Relaxation Measurements
K. Sakamoto, M. Kamiya, T. Uchida, K. Kawano, and K. Ishimori
Biochem. Biophys. Res. Commun., Vol. 398, 231-236 (2010).

4.

Global Minimum Geometries of Acetylene Clusters (HCCH)n with n ≤ 55 Obtained by a Heuristic Method Combined with Geometrical Perturbations
H. Takeuchi
J. Comput. Chem., Vol. 31, 1699-1706 (2010).

5.

Molecular Oxygen Regulates the Enzymatic Activity of a Heme-containing Diguanylate Cyclase (HemDGC) for the Synthesis of Cyclic di-GMP
H. Sawai, S. Yoshioka, T. Uchida, M. Hyodo, Y. Hayakawa, K. Ishimori, and S.
Aono
Biochim. Biophys. Acta, Vol. 1804, 166-172 (2010).

 

2009

1.

Optical Manipulation of Proteins in Aqueous Solution
Y. Tsuboi, T. Shoji, M. Nishino, S. Masuda, K. Ishimori, and N. Kitamura
App. Sur. Sci., Vol. 255, 9906–9908 (2009)

To Page top