研究者詳細 - 荘司　長三

論文 - 荘司　長三

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Activation of Wild-type Cytochrome P450BM3 by the Next Generation of Decoy Molecules: Enhanced Hydroxylation of Gaseous Alkanes and Crystallographic Evidence 査読有り

Z. Cong, O. Shoji, C. Kasai, N. Kawakami, H. Sugimoto, Y. Shiro, Y. Watanabe

ACS Catalysis 5 巻頁： 150–156 2015年1月

Bringing out the potential of wild-type cytochrome P450s using decoy molecules: Oxygenation of nonnative substrates by bacterial cytochrome P450s 査読有り

O. Shoji, Y. Watanabe

Isr. J. Chem. 55 巻 ( 1 ) 頁： 32–39 2015年1月

GluN2B-Selective N-Methyl-d-aspartate (NMDA) Receptor Antagonists Derived from 3-Benzazepines: Synthesis and Pharmacological Evaluation of Benzo[7]annulen-7-amines 査読有り

A. Benner, A. Bonifazi, C. Shirataki, L. Temme, D. Schepmann, W. Quaglia, O. Shoji, Y. Watanabe, C. Daniliuc, B. Wünsch

ChemMedChem 9 巻 ( 4 ) 頁： 741-751 2014年4月

Inhibition of Heme Uptake in Pseudomonas aeruginosa by its Hemophore (HasAp) Bound to Synthetic Metal Complexes 査読有り

C. Shirataki, O. Shoji, M. Terada, S. Ozaki, H. Sugimoto, Y. Shiro, Y. Watanabe

Angew. Chem. Int. Ed. 53 巻頁： 2862-2866 2014年3月

Peroxygenase reactions catalyzed by cytochromes P450 査読有り

O. Shoji, Y. Watanabe

J. Biol. Inorg. Chem 19 巻 ( 4-5 ) 頁： 529-539 2014年2月

Electronic Control of Discrimination between O2 and CO in Myoglobin Lacking the Distal Histidine Residue 査読有り

R. Nishimura, T. Shibata, I. Ishigami, T. Ogura, H. Tai, S. Nagao, T. Matsuo, S Hirota, O. Shoji, Y. Watanabe, K. Imai, S. Neya, A. Suzuki, Y. Yamamoto

Inorg. Chem 53 巻頁： 1091–1099 2013年12月

Highly Selective Hydroxylation of Benzene to Phenol by Wild-type Cytochrome P450BM3 Assisted by Decoy Molecules 査読有り

O. Shoji, T. Kunimatsu, N. Kawakami, Y. Watanabe

Angew. Chem. Int. Ed. 52 巻頁： 6606-6610 2013年6月

Direct hydroxylation of primary carbons in small alkanes by wild-type cytochrome P450BM3 containing perfluorocarboxylic acids as decoy molecules 査読有り

N. Kawakami, O. Shoji, Y. Watanabe

Chem. Sci. 4 巻頁： 2344-2348 2013年3月

Chiral-Substrate-Assisted Stereoselective Epoxidation Catalyzed by H2O2-Dependent Cytochrome P450SPα 査読有り

T. Fujishiro, O. Shoji, N. Kawakami, T. Watanabe, H. Sugimoto, Y. Shiro, Y. Watanabe

Chemistry-An Asian Journal 7 巻 ( 10 ) 頁： 2286-2293 2012年10月

Single-step reconstitution of apo-hemoproteins at the disruption stage of Escherichia coli cells 査読有り

N. Kawakami, O. Shoji, Y.Watanabe

ChemBioChem 13 巻 ( 14 ) 頁： 2045-2047 2012年9月

Construction of Biocatalysts Using the Myoglobin Scaffold for the Synthesis of Indigo from Indole 査読有り

J. Xu, O. Shoji, T. Fujishiro, T. Ohki, T. Ueno, Y. Watanabe

Catalysis Science & Technology 2 巻頁： 739-744 2012年4月

Molecular Design of Heme Proteins for Future Application 査読有り

H. Nakajima, O. Shoji, Y. Watanabe

Catalysis Surveys from Asia 15 巻 ( 3 ) 頁： 134-143 2011年6月

記述言語：英語掲載種別：研究論文（学術雑誌）

This review surveys our recent studies on artificial heme oxygenases, which consists of two topics. The first topic is an artificial peroxidase founded on a thermally tolerant protein, which shows high thermal stability in the catalytic reaction. In the second topic, we describe `Decoy system' that has been developed to transform Cytochrome P450BSβ into a versatile oxygenase.

Crystal structure of H2O2-dependent cytochrome P450SPα with its bound fatty acid substrate: insight into the regioselective hydroxylation of fatty acids at the α position 査読有り

T. Fujishiro, O. Shoji, S. Nagano, H. Sugimoto, Y. Shiro, Y. Watanabe

J. Biol. Chem. 286 巻頁： 29941-29950 2011年6月

Use of Perfluoro Carboxylic Acids Trick Cytochrome P450BM3 into Initiating Hydroxylation of Gaseous Alkanes 査読有り

N. Kawakami, O. Shoji, Y. Watanabe

Angew.Chem.Int.Ed 50 巻頁： 5315-5318 2011年4月

Design of H2O2-Dependent Oxidation Catalyzed by Hemoproteins 査読有り

O. Shoji, Y. Watanabe

Metallomics 3 巻頁： 379-388 2011年2月

担当区分：筆頭著者記述言語：英語掲載種別：研究論文（学術雑誌）

The monooxygenese activity of cytochrome P450 is successfully introduced into myoglobin by rational design of its active site. Introduction of an aromatic ring, tryptophan, near the heme by site-directed mutagenesis resulted in the hydroxylation of tryptophan at the C6 position by using an almost stoichiometric amount of H(2)O(2). We also altered the substrate specificity of H(2)O(2)-dependent P450 by employing a simple substrate trick. Although P450(BSβ) exclusively catalyzes peroxygenation of long-alkyl-chain fatty acids, oxidation of non-natural substrates such as styrene, ethylbenzene, and 1-methoxynaphthalen are catalyzed by P450(BSβ) in the presence of decoy molecules having a carboxyl group. Advantageously, the substrate specificity of P450(BSβ) can be altered by simply adding the decoy molecule without replacing any amino acid residues. Moreover, the stereoselectivity can be controlled by changing the structure of the decoy molecule. The crystal structure analysis of the decoy molecule bound-form of P450(BSβ) shows that P450(BSβ) accepts the decoy molecule, whose carboxylate is located at the same position to that of long-alkyl-chain fatty acid.

Non-covalent modification of the active site of cytochrome P450 for inverting the stereoselectivity of monooxygenation 査読有り

Takashi Fujishiro, Osami Shoji, Yoshihito Watanabe

Tetrahedron Letters 53 巻 ( 3 ) 頁： 395-397 2010年12月

記述言語：英語掲載種別：研究論文（学術雑誌）

The enantioselectivity in the sulfoxidation of thioanisole catalyzed by cytochrome P450BSβ with a decoy molecule, a dummy molecule of the natural substrate, can be inverted by changing the structure of the decoy molecule. The methodology demonstrated herein shows the potential for controlling the stereoselectivity of biocatalysts without any mutagenesis.

Understanding substrate misrecognition of hydrogen peroxide dependent cytochrome P450 from Bacillus subtilis 査読有り

Osami Shoji, Takashi Fujishiro, Shingo Nagano, Shota Tanaka, Takuya Hirose, Yoshitsugu Shiro, Yoshihito Watanabe

J. Biol. Inorg. Chem. 15 巻 ( 8 ) 頁： 1331-1339 2010年8月

担当区分：筆頭著者記述言語：英語掲載種別：研究論文（学術雑誌）

Cytochrome P450(BSβ), a H(2)O(2)-dependent cytochrome P450 catalyzing the hydroxylation of long-alkyl-chain fatty acids, lacks the general acid-base residue around the heme, which is indispensable for the efficient generation of the active species using H(2)O(2). On the basis of the crystal structure of the palmitic acid bound form of cytochrome P450(BSβ), it was suggested that the role of the general acid-base function was provided by the carboxylate group of fatty acids. The participation of the carboxylate group of the substrate was supported by the fact that cytochrome P450(BSβ) can catalyze oxidations of nonnatural substrates such as styrene and ethylbenzene in the presence of a series of short-alkyl-chain carboxylic acids as a dummy molecule of fatty acid. We refer to a series of short-alkyl-chain carboxylic acids as a "decoy molecule". As shown here, we have clarified the crystal structure of the decoy-molecule-bound form and elucidated that the location of its carboxylate group is virtually the same as that of palmitic acid in the heme cavity, indicating that the carboxylate group of the decoy molecule serves as the general acid-base catalyst. This result further confirms that the role of the acid-base function is satisfied by the carboxylate group of the substrates. In addition, the structure analysis of the substrate-free form has clarified that no remarkable structural change is induced by the binding of the decoy molecule as well as fatty acid. Consequently, whether the carboxylate group is positioned in the active site provides the switching mechanism of the catalytic cycle of cytochrome P450(BSβ).

Aromatic C-H bond hydroxylation by P450 peroxygenases: a facile colorimetric assay for monooxygenation activities of enzymes based on Russig's blue formation 査読有り

Osami Shoji, Christian Wiese, Takashi Fujishiro, Chikako Shirataki, Bernhard Wünsch, Yoshihito Watanabe

J. Biol. Inorg. Chem. 15 巻 ( 7 ) 頁： 1109-1115 2010年5月

担当区分：筆頭著者記述言語：英語掲載種別：研究論文（学術雑誌）

Aromatic C-H bond hydroxylation of 1-methoxynaphthalene was efficiently catalyzed by the substrate misrecognition system of the hydrogen peroxide dependent cytochrome P450BSβ (CYP152A1), which usually catalyzes hydroxylation of long-alkyl-chain fatty acids. Very importantly, the hydroxylation of 1-methoxynaphthalene can be monitored by a color change since the formation of 4-methoxy-1-naphthol was immediately followed by its further oxidation to yield Russig's blue. Russig's blue formation allows us to estimate the peroxygenation activity of enzymes without the use of high performance liquid chromatography, gas chromatography, and nuclear magnetic resonance measurements.

Hydrogen Peroxide-Dependent Monooxygenations by Tricking the Substrate Recognition of Cytochrome P450BSb 査読有り

Osami Shoji, Takashi Fujishiro, Hiroshi Nakajima, Misa Kim, Shingo Nagano, Yoshitsugu Shiro, Yoshihito Watanabe

Angew. Chem. Int. Ed. 46 巻 ( 20 ) 頁： 3656-3659 2007年5月

Supramolecular array of imizazolylethynyl-zinc-porphyrin 査読有り

Akiharu Satake, Osami Shoji, Yoshiaki Kobuke

J. Organomet. Chem. 692 巻 ( 1-3 ) 頁： 635-644 2006年8月

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