模拟自然界的金属介导反应

Stephan Diekmann , Jennie Weston , Ernst Anders , Wilhelm Boland , Bruno Schönecker , Thomas Hettmann , Johannes von Langen , Stefan Erhardt , Michael Mauksch , Michael Bräuer , Christoph Beckmann , Matthias Rost , Petra Sperling , Ernst Heinz
{"title":"模拟自然界的金属介导反应","authors":"Stephan Diekmann ,&nbsp;Jennie Weston ,&nbsp;Ernst Anders ,&nbsp;Wilhelm Boland ,&nbsp;Bruno Schönecker ,&nbsp;Thomas Hettmann ,&nbsp;Johannes von Langen ,&nbsp;Stefan Erhardt ,&nbsp;Michael Mauksch ,&nbsp;Michael Bräuer ,&nbsp;Christoph Beckmann ,&nbsp;Matthias Rost ,&nbsp;Petra Sperling ,&nbsp;Ernst Heinz","doi":"10.1016/S1389-0352(01)00067-8","DOIUrl":null,"url":null,"abstract":"<div><p><span>The Collaborative Research Center (CRC) 436 ‘Metal-Mediated Reactions Modeled after Nature’ was founded for the express purpose of analyzing the catalytic principles of metallo-enzymes in order to construct efficient catalysts on a chemical basis. The structure of the active center and neighboring chemical environment in enzymes serves as a focal point for developing reactivity models for the chemical redesign of catalysts. Instead of simply copying enzyme construction, we strive to achieve new chemical intuition based on the results of long-lasting natural evolution. We hope for success, since nature uses a limited set of building blocks, whereas we can apply the full repertoire of chemistry. Key substrates in this approach are small molecules, such as CO</span><sub>2</sub>, O<sub>2</sub>, NO<sub>3</sub><sup>−</sup> and N<sub>2</sub><span>. Nature complexes these substrates, activates them and performs chemical transformations — all within the active center of a metalloenzyme. In this article, we report on some aspects and first results of the Collaborative Research Center (CRC) 436, such as nitrate reductase<span>, sphingolipid<span> desaturase, carbonic anhydrase<span>, leucine<span> aminopeptidase and dopamine β-monooxygenase.</span></span></span></span></span></p></div>","PeriodicalId":101090,"journal":{"name":"Reviews in Molecular Biotechnology","volume":"90 2","pages":"Pages 73-94"},"PeriodicalIF":0.0000,"publicationDate":"2002-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S1389-0352(01)00067-8","citationCount":"9","resultStr":"{\"title\":\"Metal-mediated reactions modeled after nature\",\"authors\":\"Stephan Diekmann ,&nbsp;Jennie Weston ,&nbsp;Ernst Anders ,&nbsp;Wilhelm Boland ,&nbsp;Bruno Schönecker ,&nbsp;Thomas Hettmann ,&nbsp;Johannes von Langen ,&nbsp;Stefan Erhardt ,&nbsp;Michael Mauksch ,&nbsp;Michael Bräuer ,&nbsp;Christoph Beckmann ,&nbsp;Matthias Rost ,&nbsp;Petra Sperling ,&nbsp;Ernst Heinz\",\"doi\":\"10.1016/S1389-0352(01)00067-8\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p><span>The Collaborative Research Center (CRC) 436 ‘Metal-Mediated Reactions Modeled after Nature’ was founded for the express purpose of analyzing the catalytic principles of metallo-enzymes in order to construct efficient catalysts on a chemical basis. The structure of the active center and neighboring chemical environment in enzymes serves as a focal point for developing reactivity models for the chemical redesign of catalysts. Instead of simply copying enzyme construction, we strive to achieve new chemical intuition based on the results of long-lasting natural evolution. We hope for success, since nature uses a limited set of building blocks, whereas we can apply the full repertoire of chemistry. Key substrates in this approach are small molecules, such as CO</span><sub>2</sub>, O<sub>2</sub>, NO<sub>3</sub><sup>−</sup> and N<sub>2</sub><span>. Nature complexes these substrates, activates them and performs chemical transformations — all within the active center of a metalloenzyme. In this article, we report on some aspects and first results of the Collaborative Research Center (CRC) 436, such as nitrate reductase<span>, sphingolipid<span> desaturase, carbonic anhydrase<span>, leucine<span> aminopeptidase and dopamine β-monooxygenase.</span></span></span></span></span></p></div>\",\"PeriodicalId\":101090,\"journal\":{\"name\":\"Reviews in Molecular Biotechnology\",\"volume\":\"90 2\",\"pages\":\"Pages 73-94\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2002-04-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S1389-0352(01)00067-8\",\"citationCount\":\"9\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Reviews in Molecular Biotechnology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1389035201000678\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Reviews in Molecular Biotechnology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1389035201000678","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 9

摘要

合作研究中心(CRC) 436“模拟自然的金属介导反应”的成立是为了明确分析金属酶的催化原理,以便在化学基础上构建有效的催化剂。酶活性中心的结构和邻近的化学环境是建立催化剂化学再设计的反应性模型的重点。我们不是简单地复制酶的结构,而是基于长期自然进化的结果,努力实现新的化学直觉。我们希望成功,因为大自然使用的是一套有限的积木,而我们可以应用化学的全部技能。这种方法的关键底物是小分子,如CO2、O2、NO3−和N2。大自然使这些底物复合物,激活它们并进行化学转化——所有这些都在金属酶的活性中心内进行。本文报道了CRC 436合作研究中心在硝酸盐还原酶、鞘脂去饱和酶、碳酸酐酶、亮氨酸氨基肽酶和多巴胺β-单加氧酶等方面的研究成果。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
Metal-mediated reactions modeled after nature

The Collaborative Research Center (CRC) 436 ‘Metal-Mediated Reactions Modeled after Nature’ was founded for the express purpose of analyzing the catalytic principles of metallo-enzymes in order to construct efficient catalysts on a chemical basis. The structure of the active center and neighboring chemical environment in enzymes serves as a focal point for developing reactivity models for the chemical redesign of catalysts. Instead of simply copying enzyme construction, we strive to achieve new chemical intuition based on the results of long-lasting natural evolution. We hope for success, since nature uses a limited set of building blocks, whereas we can apply the full repertoire of chemistry. Key substrates in this approach are small molecules, such as CO2, O2, NO3 and N2. Nature complexes these substrates, activates them and performs chemical transformations — all within the active center of a metalloenzyme. In this article, we report on some aspects and first results of the Collaborative Research Center (CRC) 436, such as nitrate reductase, sphingolipid desaturase, carbonic anhydrase, leucine aminopeptidase and dopamine β-monooxygenase.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
Subject Index Author Index Core and periphery functionalized dendrimers for transition metal catalysis; a covalent and a non-covalent approach Dendritic supports in organic synthesis Peptide dendrimers: applications and synthesis
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1