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| Murakawa T, Suzuki M, Fukui K, et al. (2022) Serial femtosecond X-ray crystallography of an anaerobically formed catalytic intermediate of copper amine oxidase. Acta Crystallographica. Section D, Structural Biology. 78: 1428-1438 |
| Shoji M, Murakawa T, Nakanishi S, et al. (2022) Molecular mechanism of a large conformational change of the quinone cofactor in the semiquinone intermediate of bacterial copper amine oxidase. Chemical Science. 13: 10923-10938 |
| Murakawa T, Kurihara K, Adachi M, et al. (2022) Re-evaluation of protein neutron crystallography with and without X-ray/neutron joint refinement. Iucrj. 9: 342-348 |
| Murakawa T, Suzuki M, Arima T, et al. (2021) Microcrystal preparation for serial femtosecond X-ray crystallography of bacterial copper amine oxidase. Acta Crystallographica. Section F, Structural Biology Communications. 77: 356-363 |
| Oozeki T, Nakai T, Kozakai K, et al. (2021) Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor. Nature Communications. 12: 933 |
| Shoji M, Murakawa T, Boero M, et al. (2020) Unique protonation states of aspartate and topaquinone in the active site of copper amine oxidase. Rsc Advances. 10: 38631-38639 |
| Murakawa T, Kurihara K, Shoji M, et al. (2020) Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing. Proceedings of the National Academy of Sciences of the United States of America. 117: 10818-10824 |
| Murakawa T, Baba S, Kawano Y, et al. (2019) thermodynamic analysis of conformational change of the topaquinone cofactor in bacterial copper amine oxidase. Proceedings of the National Academy of Sciences of the United States of America. 116: 135-140 |
| Murakawa T, Hamaguchi A, Nakanishi S, et al. (2015) Probing the Catalytic Mechanism of Copper Amine Oxidase from Arthrobacter globiformis with Halide Ions. The Journal of Biological Chemistry. 290: 23094-109 |
| Nakai T, Ito H, Kobayashi K, et al. (2015) The Radical S-Adenosyl-L-methionine Enzyme QhpD Catalyzes Sequential Formation of Intra-protein Sulfur-to-Methylene Carbon Thioether Bonds. The Journal of Biological Chemistry. 290: 11144-66 |