Monolayer Protected Nanoparticles Flavoenzyme Models

单层保护纳米粒子黄素酶模型

• 批准号: 6948617
• 负责人: VINCENT M. ROTELLO
• 金额: $ 21.16万
• 依托单位: UNIVERSITY OF MASSACHUSETTS AMHERST
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-04-01 至 2006-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6948617
• 关键词: active sites; chemical group; chemical models; cofactor; electron nuclear double resonance spectroscopy; electron spin resonance spectroscopy; electron transport; enzyme activity; enzyme mechanism; enzyme model; enzyme structure; enzyme substrate; flavins; flavoproteins; model design /development; molecular assembly /self assembly; molecular film; nuclear magnetic resonance spectroscopy; oxidation reduction reaction; oxidoreductase; structural biology; synthetic enzyme

DESCRIPTION: (provided by applicant) Site isolation and presentation of functionality are two key requirements for enzymatic catalysis. Researchers have developed synthetic systems that effectively mimic either the functionality or the isolation of enzyme active sites; creation of constructs that provide both of these attributes remains a significant challenge. We will use self-assembled monolayers (SAMs) on monolayer-protected gold clusters (MMPCs) to provide both the isolation and preorganization required to effectively replicate the behavior of flavoenzyme systems. There are three key thrusts to our proposed research: 1) The effective duplication of enzyme-cofactor interactions using the preorganization provided by the SAM, coupled with the control provided by the radial nature of the MMPC sidechains. 2) Fabrication of MMPC structures that provide effective isolation of cofactors buried within the SAM from solvent and other interfering species. 3) We will combine expertise gained from the above programs to design and fabricate fully functional mimics of the electron transferase family of flavoenzymes. These investigations will address key issues of recognition in water and control of enzyme mimic redox potentials, and will culminate with the creation of a functional electron shuttle designed to fully replicate the function of an electron transferase.

描述：（由申请人提供）研究中心隔离和 功能性是酶催化的两个关键要求。研究人员 已经开发出了合成系统，可以有效地模仿 功能或酶活性位点的分离;构建体的产生 同时提供这两种属性仍然是一个重大的挑战。我们将 在单层保护的金簇上使用自组装单分子层（SAM） （MMPC）提供所需的隔离和预组织， 有效地复制了黄素酶系统的行为。有三个关键 我们提议的研究的重点： 1)酶-辅因子相互作用的有效复制， 由SAM提供的预组织，再加上由 MMPC侧链的径向性质。 2)提供辅因子的有效隔离的MMPC结构的制造 从溶剂和其他干扰物质中去除SAM。 3)我们将结合联合收割机的专业知识，从上述方案中获得的设计和 制造电子转移酶家族的全功能模拟物， 黄素酶这些调查将解决承认的关键问题， 水和酶的控制模拟氧化还原电位，并将达到高潮， 创造一个功能性的电子穿梭机，旨在完全复制 电子转移酶的功能。

项目成果

Model systems for flavoenzyme activity: a tuneable intramolecularly hydrogen bonded flavin-diamidopyridine complex.

• DOI: 10.1039/b501887k
• 发表时间: 2005-05
• 期刊: Chemical communications
• 影响因子: 4.9
• 作者: A. Boyd;J. B. Carroll;G. Cooke;James F. Garety;Brian J. Jordan;Suhil Mabruk;G. Rosair;V. Rotello

Model systems for flavoenzyme activity: an electrochemically tuneable model of roseoflavin.

• DOI: 10.1039/b401470g
• 发表时间: 2004-04
• 期刊: Chemical communications
• 影响因子: 4.9
• 作者: G. Cooke;Y. Legrand;V. Rotello

The electrochemically-tuneable interactions between flavin-functionalised C60 derivatives and 2,6-diethylamidopyridine.

• DOI: 10.1039/b505215g
• 发表时间: 2005-07
• 期刊: Chemical communications
• 影响因子: 4.9
• 作者: J. B. Carroll;G. Cooke;James F. Garety;Brian J. Jordan;Suhil Mabruk;V. Rotello

Hydrogen bonding in redox-modulated molecular recognition. An experimental and theoretical investigation.

• DOI: 10.1021/ja035228b
• 发表时间: 2003-06
• 期刊: Journal of the American Chemical Society
• 影响因子: 15
• 作者: M. Gray;A. O. Cuello;G. Cooke;V. Rotello

Model systems for flavoenzyme activity. Control of flavin recognition via specific electrostatic interactions.

• DOI: 10.1021/ol015838l
• 发表时间: 2001-04
• 期刊: Organic letters
• 影响因子: 5.2
• 作者: A. Goodman;E. Breinlinger;C. M. McIntosh;L. Grimaldi;V. Rotello