COPPER AND IRON DIOXYGEN REACTIVITY IN MODEL COMPLEXES

描述：（改编自申请人的摘要）独特的生物运动 对小的合成分子的催化反应性，而一个强大的 挑战，是一个非常有趣和翔实的奋进，提供 对天然反应性的重要见解。广泛和长期的目标 的结构和电子性质的阐明， 生物单核、双核和三核中形成的Cu-O2物种 Cu位点及其氧化反应性的后续表征。的 方法是合成类似物的方法的活性位点的 金属生物分子，由此合成低分子量络合物， 在小分子水平上进行详细检查，以揭示 金属络合物从蛋白质基质的影响中解偶联。的 前提是生物的形成和随后的反应性 中间体在小的合成复合物中应该是可再现的， 适当的连接环境被工程化，并且如果是有害的， 避免了活性中间体的双分子反应。创建 光谱一致的功能模型是最终目标， 提出的生物学机制的具体方面可以在一个 小分子细节水平。具体目标如下： [Cu（I）LDAL（MeCN）]1+-O2光谱和反应性表征 使用简单的全烷基化二胺配体（LDA）的产品， 可能的生物中间体和光谱基准的优先顺序 由此可以鉴定这些中间体。反应性表征 新的中间体可以产生新的生物激发的氧化催化剂。限定 半乳糖氧化酶催化功能机理关系 模型复杂到本地系统。开发更耐氧化的 模型复合物将有助于机理和动力学研究。一体化 组氨酸终止的肽进入配体框架将提供更多的 半乳糖氧化酶的生物学相关功能模型。功能 模拟单核三角连接铜位点与 研究促进O2活化的环境类型， Cu-O2中间体的形成及酚基氧化机理 修饰，单核铜酶的一个新兴主题。发展 脂氧合酶，一种单核铁酶， 单核铁模型表现出与CH最一致的氧化行为， 氢原子抽象。

DESCRIPTION: (adapted from applicant's abstract) Movement of unique biological catalytic reactivity to small synthetic molecules, while a formidable challenge, is an extremely intriguing and informative endeavor providing critical insights into the native reactivity. The broad and long-term objective of this research is elucidation of the structural and electronic properties of Cu-O2 species formed in biological mononuclear, binuclear and trinuclear Cu-sites and subsequent characterization of their oxidative reactivity. The methodology is that of the synthetic analog approach to the active sites of metallobiomolecules, whereby low molecular weight complexes are synthesized and examined at a small molecule level of detail to reveal intrinsic properties of the metal complexes uncoupled from the influences of the protein matrix. The premise is that the formation and subsequent reactivity of biological intermediates should be reproducible in small synthetic complexes if appropriate ligation environments are engineered, and if deleterious bimolecular reactions of the reactive intermediates are avoided. Creation of spectroscopically congruent, functional models is the ultimate goal so that specific aspects of proposed biological mechanisms may be investigated at a small molecule level of detail. The specific aims are as follows: Structural, spectroscopic and reactivity characterization of [Cu(I)LDAL(MeCN)]1+-O2 products using simple peralkylated diamines ligands (LDA) to provide chemical precedence for possible biological intermediates and spectroscopic benchmarks by which such intermediates may be identified. Reactivity characterization of new intermediates may lead to new bio-inspired oxidation catalysts. Defining the mechanistic relationship of catalytically functional galactose oxidase model complexes to the native system. Development of more oxidatively resistant model complexes will aid in the mechanistic and kinetic studies. Integration of histidine terminated peptides into the ligand framework will provide more biologically relevant functional models of galactose oxidase. Functional modeling of the reactivity of mononuclear trigonally-ligated copper sites to investigate the type of environments that promote O2 activation, the type of Cu-O2 intermediates formed, and the mechanism of phenolate group oxidative modification, an emerging theme in mononuclear copper enzymes. Development of a mechanistic relationship between lipoxygenase, a mononuclear iron enzyme, and mononuclear iron models that exhibit oxidation behavior most consistent with CH hydrogen atom abstraction.