1P096 Heme serves as scaffold for substrate-driven active site structuring in cytochrome P450cam(02. Heme proteins,Poster)

スポンサーリンク

概要

著者

関連論文

1I1636 完全酸化型ウシ心筋チトクロム酸化酵素の吸収スペクトルへの結晶化、及び凍結防止処理の影響(ヘム蛋白質 1,第49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)
2PT155 cbb_3型チトクロム酸化酵素の酸素消費活性(日本生物物理学会第50回年会(2012年度))
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)

もっと見る

スポンサーリンク