U.S.-Italy Cooperative Research: Biophysical Characterization of Type 3 Copper Sites

该奖项将支持叶史瓦大学Jack Peisach教授和意大利帕多瓦大学Benedetto Salvato博士之间的合作研究。研究人员的目标是使用各种光谱技术研究铜蛋白的结构，以确定和控制生物功能。铜是最广泛和最通用的过渡金属之一，在生命系统中具有功能作用。许多与氧传递、电子传递、羟基化和氧化催化等生物学功能相关的金属蛋白都以某种方式与铜有关。铜蛋白具有一个共同的结构特征，使它们能够改变活性位点的极性，控制底物的水合作用，并在催化过程中发挥重要作用。然而，铜蛋白在分子结构的复杂性以及它们的酶催化机制方面差异很大。然而，铜位点可根据其光谱特性分为三大类。研究人员计划研究这些类别之一（3型铜位点）以及这些位点在与多铜酶中其他铜中心相互作用期间的行为。该研究计划将涉及对血蓝蛋白、漆酶和血浆铜蓝蛋白的研究，这些蛋白在不同的分子环境中含有3型铜单位，具有不同的酶活性。帕多瓦的血蓝蛋白研究小组是这种蛋白质比较研究的领先中心之一，在其物理，生物和生物物理化学方面具有综合专业知识，而在叶史瓦大学，有独特的仪器和专业知识，可以从光谱方法获得的信息中阐明结构。

This award will support collaborative research between Prof. Jack Peisach of Yeshiva University and Dr. Benedetto Salvato of the University of Padova, Italy. The objective of the researchers is to study, using various spectroscopic techniques, the structure of copper proteins in the determination and control of biological functions. Copper is one of the most widespread and versatile transition metals with a functional role in living systems. Many metallo-proteins related to a variety of biological functions such as oxygen transport, electron transfer, hydroxylation and oxidative catalysis, involve copper in some manner. Copper proteins share a general structural feature that allows them to modify the polarity of active sites, control the hydration of substrates, and play an important role during the course of catalysis. Yet, copper proteins vary widely in complexity of molecular architecture as well as in their mechanism of enzyme catalysis. However, copper sites may be classified into three broad categories depending on their spectroscopic characteristics. The investigators plan to study one of these categories (Type 3 copper sites) and the behavior of these sites during the interactions with other copper centers in multi-copper enzymes. The research program will involve the study of hemocyanin, laccase and ceruloplasmin, which contain Type 3 copper units in different molecular environments and have different enzymatic activities. The hemocyanin research group in Padova is one of the leading centers for the comparative study of this protein, having combined expertise in its physical, biological and biophysical chemistry, whereas at Yeshiva University there is unique instrumentation and expertise relevant to elucidation of structure from information obtainable by spectroscopic methods.