Kinetics and Mechanisms of Photoinduced Electron-Transfer Reaction of Zinc Myoglobin. Intracomplex vs. Intermolecular Quenching Controlled by Conformational Change Associated with Charge and Steric Bulk of Quenchers
Kinetics and Mechanisms of Photoinduced Electron-Transfer Reaction of Zinc Myoglobin. Intracomplex vs. Intermolecular Quenching Controlled by Conformational Change Associated with Charge and Steric Bulk of Quenchers
复制标题
锌肌红蛋白光致电子转移反应的动力学和机制。
DOI：
--
复制
发表时间：
1994
期刊：
影响因子：
--
通讯作者：
T. Sakurai
中科院分区：
文献类型：
--
作者：
K. Tsukahara;S. Asami;Mihoko Okada;T. Sakurai
在脱气水溶液中，研究了锌肌红蛋白（ZnPPMb）与各种猝灭剂(如六氰高铁酸盐（III） （[Fe(CN)6]3−）和六胺矿铀（III） （[Ru（NH3)6]3+）离子、阳离子致红剂、铜（II）蛋白（星青苷）和甲肌红蛋白）之间的光致电子转移（ET）。ZnPPMb （*ZnPPMb）在自结合配合物中被[Fe(CN)6]3−猝灭。随着离子强度的增大，自缔合物的猝灭速率常数和形成常数均减小。未观察到该体系的热反向ET反应；极有可能的是，反向ET反应比猝灭反应快得多。本研究中检测的所有阳离子猝灭剂都没有与*ZnPPMb形成自结合的配合物，并且发生了分子间猝灭。观察了这些阳离子猝灭剂的热反向ET反应。光诱导ET和热反向ET反应对驱动力不敏感。
Photoinduced electron transfer (ET) between zinc myoglobin (ZnPPMb) and a variety of quenchers, such as hexacyanoferrate(III) ([Fe(CN)6]3−) and hexaammineruthenium(III) ([Ru(NH3)6]3+) ions, cationic viologens, copper(II) protein (stellacyanin), and metmyoglobins, has been studied in aqueous degassed solutions. The excited triplet state of ZnPPMb (*ZnPPMb) was quenched by [Fe(CN)6]3− in a self-associated complex. Both quenching rate constant and formation constant of the self-associated complex decrease with increasing ionic strengths. The thermal backward ET reaction for this system was not observed; it is most likely that the backward ET step is much faster than the quenching reaction. All of the cationic quenchers examined in this work did not form a self-associated complex with *ZnPPMb, and the intermolecular quenching occurred. The thermal backward ET reaction was observed for these cationic quenchers. Not only photoinduced ET but also thermal backward ET reactions were insensitive to the driving forc...
小分子通过血红蛋白结构的迁移：蛋白质电子转移反应中门控的证据。
影响因子：
2.9
作者：
Feitelson,J;McLendon,G
通讯作者：
McLendon,G