Influences of the Hydrophobicity of the Heme-binding Pocket on the Properties and Functions of Cytochrome b_5 Mutants

IntroductionElectrontransferreactionsarethekeystepsinphoto synthesis ,respirationandmanyotherbiochemicalprocess es.1Cytochromeb5isaredoxproteinexistingwidelyinnature ,whichactsasanelectron carrierduringvariouselectrontransferprocessesinthebiologicalsystem .2Cytochromeb5isamembraneproteinwithmolecularweightofapproximately 16kDa ,ofwhichthehydrophobicC terminaldomainanchorscytochromeb5tothemem brane ,andthehydrophilicN terminaldomaincontainshemeprostheticgroupandexhibitsthebiologicalfunctionsof…     

铯饱和吸收光谱随抽运光强度的变化

研究了铯饱和吸收光谱随抽运光强度变化的情况，特别是６^２Ｓ_１／２Ｆ＝４→６^２Ｐ_３／２Ｆ′＝５的谱线的变化行为．在线偏振光抽运、线偏振光检测的情况下，计入所有相关的Ｚｅｅｍａｎ子能级之间的跃迁，考虑光抽运与饱和效应的共同作用，运用Ｒｕｎｇｅ-Ｋｕｔａ法则求解粒子数方程，计算得出的饱和吸收谱与实验结果符合得较好．还给出了较直观的物理解释 关键词：     

激光冷却与囚禁的原子喷泉

本文介绍了激光冷却与囚禁的原子喷泉的主要环节，首先介绍了与原子喷泉有密切关系的光学粘团和原子阱的原理和结构，然后介绍了原子喷泉的实验装置、实验步骤和实验结果。     

Influences of the Hydrophobicity of the Heme－binding Pocket on the Properties and Functions of Cytochrome b5 Mutants

The mutation sites of the four mutants F35Y, P40V, V45E and V45Y of cytochrome b5 are located at the edge of the heme-binding pocket. The solvent accessible areas of the “pocket inte-rior“ of the four mutants and the wild-type cytochrome b5 have been calculated based on their crystal structures at high resolu-tion. The change in the hydrophobicity of the heme-binding pocket resulting from the mutation can be quantitatively de-scribed using the difference of the solvent accessible area of the “pocket interior“ of each mutant from that of the wild-type cy-tochrome b5. The influences of the hydrophobicity of the heme-binding pocket on the protein stability and redox potential are discussed.     

@—激光冷却与囚禁的原子喷泉

本文介绍了激光冷却与囚禁的原子喷泉的主要环节，首先介绍了与原子喷泉有密切关系的光学粘团和原子的原理和结构，然后介绍了原子喷泉的实验装置、实验步骤和实验结果。     

Structures of Cytochrome b_5 Mutated at the Charged Surface-Residues and Their Interactions with Cytochrome c

ＩｎｔｒｏｄｕｃｔｉｏｎＭｉｃｒｏｓｏｍａｌｃｙｔｏｃｈｒｏｍｅｂ5(Ｃｙｔｂ5)ｉｓａｍｅｍｂｅｒｏｆｃｙｔｏｃｈｒｏｍｅｂ5ｆａｍｉｌｙ ,ａｎｄｉｔｓｅｒｖｅｓａｓａｎｅｌｅｃｔｒｏｎｃａｒｒｉｅｒｉｎａｓｅｒｉｅｓｏｆｅｌｅｃｔｒｏｎ ｔｒａｎｓｆｅｒｐｒｏｃｅｓｓｅｓｉｎｂｉｏｌｏｇｉｃａｌｓｙｓ ｔｅｍｓ .1 3 Ｃｙｔｂ5ｉｓａｍｅｍｂｒａｎｅｐｒｏｔｅｉｎｗｉｔｈＭｒ～ 16ｋＤａ ,ｃｏｎｓｉｓｔｉｎｇｏｆｔｗｏｄｏｍａｉｎｓ ,ｏｎｅｈｙｄｒｏｐｈｏｂｉｃｄｏｍａｉｎｗｈｉｃｈａｎｃｈｏｒｓｔｈ…