1P095 Substrate access to slow substrate binding P450cam with mutation at the proposed gate for water egress/ingress from/to the active site(02. Heme proteins,Poster)
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概要
- 論文の詳細を見る
- 一般社団法人日本生物物理学会の論文
- 2013-09-13
著者
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Kishimoto Ayaka
Grad. Sch. Sci. Univ. Hyogo
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Harada Katsuyoshi
Grad. Sch. Eng. Osaka Univ.
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Hayashi Takashi
Grad. Sch. Eng. Osaka Univ.
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Mizushima Tsunehiro
Grad. Sch. Sci., Univ. Hyogo
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Sakurai Keisuke
Inst. Sci. Ind. Res., Osaka Univ.
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Takagi Kenji
Grad. Sch. Sci., Univ. Hyogo
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Shimada Hideo
Grad. Sch. Life Sci., Univ. Hyogo
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Shimada Hideo
Grad. Sch. Sci., Univ. Hyogo
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Harada Katsuyoshi
Grad. Sch. Eng., Osaka Univ.
関連論文
- 3P113 Substrate binding excludes water cluster from active site of cytochrome P450cam - mutation analysis of water expelling system(Heme proteins,The 48th Annual Meeting of the Biophysical Society of Japan)
- 3P-075 基質カンファー結合によるチトクロムP450camの構造変化(ヘム蛋白質,第47回日本生物物理学会年会)
- 3P-076 チトクロムP450camの活性部位からの水クラスター排出機構(ヘム蛋白質,第47回日本生物物理学会年会)
- 1P-121 チトクロムP450camの基質結合反応における活性部位近傍Asp297の役割(ヘム蛋白質,第46回日本生物物理学会年会)
- 1B1412 P34 ウシ心筋チトクロムc酸化酵素のX線構造が示唆するプロトン輸送経路の変異体解析(膜蛋白質1,第49回日本生物物理学会年会)
- 2I1548 Reaction of norcamphor with cytochrome P450cam mutated at the gate forming Asp297 for putative water expelling pathway(Heme proteins 2,The 48th Annual Meeting of the Biophysical Society of Japan)
- 2I1536 Water expelling pathway of cytochrome P450cam : Effect of mutation of a gate forming Asp297 to Leu on D-camphor binding(Heme proteins 2,The 48th Annual Meeting of the Biophysical Society of Japan)
- 2PT164 Norcamphor binding to cytochrome P450cam with a mutation to block pathway for the active site waters excluded by substrate(The 50th Annual Meeting of the Biophysical Society of Japan)
- 3PT129 Characterization by mutagenesis analysis of putative proton transfer pathway, D-pathway of bovine heart cytochrome c oxidase(The 50th Annual Meeting of the Biophysical Society of Japan)
- 2PT162 Exclusion of the active site waters by substrate in cytochrome P450cam(The 50th Annual Meeting of the Biophysical Society of Japan)
- 1P096 Heme serves as scaffold for substrate-driven active site structuring in cytochrome P450cam(02. Heme proteins,Poster)
- 1P095 Substrate access to slow substrate binding P450cam with mutation at the proposed gate for water egress/ingress from/to the active site(02. Heme proteins,Poster)
- 3P096 Sequencing bovine/human hybrid cytochrome c oxidase genes in HeLa cells to verify mutagenesis results disapproving D-path proton pumping(02. Heme proteins,Poster)