Johansson Ann-Louise, Chakrabarty Suman, Berthold Catrine L, Högbom Martin, Warshel Arieh, Brzezinski Peter
Department of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences, Stockholm University, Sweden.
Biochim Biophys Acta. 2011 Sep;1807(9):1083-94. doi: 10.1016/j.bbabio.2011.03.012. Epub 2011 Apr 2.
Cytochrome c oxidase (CytcO) is a membrane-bound enzyme, which catalyzes the reduction of di-oxygen to water and uses a major part of the free energy released in this reaction to pump protons across the membrane. In the Rhodobacter sphaeroides aa₃ CytcO all protons that are pumped across the membrane, as well as one half of the protons that are used for O₂ reduction, are transferred through one specific intraprotein proton pathway, which holds a highly conserved Glu286 residue. Key questions that need to be addressed in order to understand the function of CytcO at a molecular level are related to the timing of proton transfers from Glu286 to a "pump site" and the catalytic site, respectively. Here, we have investigated the temperature dependencies of the H/D kinetic-isotope effects of intramolecular proton-transfer reactions in the wild-type CytcO as well as in two structural CytcO variants, one in which proton uptake from solution is delayed and one in which proton pumping is uncoupled from O₂ reduction. These processes were studied for two specific reaction steps linked to transmembrane proton pumping, one that involves only proton transfer (peroxy-ferryl, P→F, transition) and one in which the same sequence of proton transfers is also linked to electron transfer to the catalytic site (ferryl-oxidized, F→O, transition). An analysis of these reactions in the framework of theory indicates that that the simpler, P→F reaction is rate-limited by proton transfer from Glu286 to the catalytic site. When the same proton-transfer events are also linked to electron transfer to the catalytic site (F→O), the proton-transfer reactions might well be gated by a protein structural change, which presumably ensures that the proton-pumping stoichiometry is maintained also in the presence of a transmembrane electrochemical gradient. Furthermore, the present study indicates that a careful analysis of the temperature dependence of the isotope effect should help us in gaining mechanistic insights about CytcO.
细胞色素c氧化酶(CytcO)是一种膜结合酶,它催化将双氧还原为水,并利用该反应释放的大部分自由能将质子泵过膜。在球形红细菌aa₃ CytcO中,所有泵过膜的质子以及用于O₂还原的一半质子,都是通过一条特定的蛋白质内质子途径转移的,该途径含有一个高度保守的Glu286残基。为了在分子水平上理解CytcO的功能,需要解决的关键问题分别与质子从Glu286转移到“泵位点”和催化位点的时间有关。在这里,我们研究了野生型CytcO以及两种结构CytcO变体中分子内质子转移反应的H/D动力学同位素效应的温度依赖性,其中一种变体中从溶液中摄取质子被延迟,另一种变体中质子泵浦与O₂还原解偶联。针对与跨膜质子泵浦相关的两个特定反应步骤研究了这些过程,一个步骤仅涉及质子转移(过氧 - 高铁,P→F,转变),另一个步骤中相同的质子转移序列也与向催化位点的电子转移相关(高铁 - 氧化,F→O,转变)。在理论框架内对这些反应的分析表明,更简单的P→F反应受质子从Glu286转移到催化位点的速率限制。当相同的质子转移事件也与向催化位点的电子转移相关(F→O)时,质子转移反应很可能由蛋白质结构变化控制,这大概确保了在存在跨膜电化学梯度的情况下也能维持质子泵浦化学计量。此外,本研究表明,仔细分析同位素效应的温度依赖性应有助于我们深入了解CytcO的机制。