| 查看: 3757 | 回复: 72 | |||||||||
| 【奖励】 本帖被评价57次，作者罗马里奥增加金币 44.6 个 | |||||||||
| 当前只显示满足指定条件的回帖，点击这里查看本话题的所有回帖 | |||||||||
[资源]
Acc. Chem. Res综述：除了活性位点，外部配位层对于电催化产氢以及氧化的影响
|
|||||||||
|
题目为Beyond the Active Site: The Impact of the Outer Coordination Sphere on Electrocatalysts for Hydrogen Production and Oxidation 作者为Bojana Ginovska-Pangovska , Arnab Dutta , Matthew L. Reback , John C. Linehan , and Wendy J. Shaw * Wendy J. Shaw is a Senior Research Scientist at PNNL. She received her Ph.D. from the University of Washington. Her research interests emphasize learning from nature and include understanding the contribution of an enzyme like outer coordination sphere on molecular catalysts with relevance for renewable energies and understanding protein–surface interactions for biomineralization systems. 全文10页，参考文献45篇。 具有氧化还原活化能力的金属酶在生物体系的能量转移反应中发挥着至关重要的作用。典型的例子是甲酸脱氢酶，固氮酶，一氧化碳脱氢酶以及氢化酶。这些反应对于人体非常重要，可以作为潜在的储存和使用能量反应来用于光电化学，电催化以及燃料电池等应用上。这些金属酶由具有氧化还原活化能力的金属中心构成，在这些金属点基质被活化而转化为相应的产物，这个过程伴随着电子和质子转移过程。 Redox active metalloenzymes play a major role in energy transformation reactions in biological systems. Examples include formate dehydrogenases, nitrogenases, CO dehydrogenase, and hydrogenases. Many of these reactions are also of interest to humans as potential energy storage or utilization reactions for photoelectrochemical, electrolytic, and fuel cell applications. These metalloenzymes consist of redox active metal centers where substrates are activated and undergo transformation to products accompanied by electron and proton transfer to or from the substrate. These active sites are typically buried deep within a protein matrix of the enzyme with channels for proton transport, electron transport, and substrate/product transport between the active site and the surface of the protein. In addition, there are amino acid residues that lie in close proximity to the active site that are thought to play important roles in regulating and enhancing enzyme activity. Directly studying the outer coordination sphere of enzymes can be challenging due to their complexity, and the use of modified molecular catalysts may allow us to provide some insight. There are two fundamentally different approaches to understand these important interactions. The “bottom-up” approach involves building an amino acid or peptide containing outer coordination sphere around a functional molecular catalyst, and the “top-down” approach involves attaching molecular catalyst to a structured protein. Both of these approaches have been undertaken for hydrogenase mimics and are the emphasis of this Account. Our focus has been to utilize amino acid or peptide based scaffolds on an active functional enzyme mimic for H2 oxidation and production, [Ni(PR2NR′2)2]2+. This “bottom-up” approach has allowed us to evaluate individual functional group and structural contributions to electrocatalysts for H2 oxidation and production. For instance, using amine, ether, and carboxylic acid functionalities in the outer coordination sphere enhances proton movement and results in lower catalytic overpotentials for H2 oxidation, while achieving water solubility in some cases. Amino acids with acidic and basic side chains concentrate substrate around catalysts for H2 production, resulting in up to 5-fold enhancements in rate. The addition of a structured peptide in an H2 production catalyst limited the structural freedom of the amino acids nearest the active site, while enhancing the overall rate. Enhanced stability to oxygen or extreme conditions such as strongly acidic or basic conditions has also resulted from an amino acid based outer coordination sphere. From the “top-down” approach, others have achieved water solubility and photocatalytic activity by associating this core complex with photosystem-I. Collectively, by use of this well understood core, the role of individual and combined features of the outer coordination sphere are starting to be understood at a mechanistic level. Common mechanisms have yet to be defined to predictably control these processes, but our growing knowledge in this area is essential for the eventual mimicry of enzymes by efficient molecular catalysts for practical use.  360软件小助手截图20140620084138.png |
回复此楼» 本帖附件资源列表
-
欢迎监督和反馈：小木虫仅提供交流平台，不对该内容负责。
本内容由用户自主发布，如果其内容涉及到知识产权问题，其责任在于用户本人，如对版权有异议，请联系邮箱：xiaomuchong@tal.com - 附件 1 : 2014-ar5001742Beyond_the_Active_Site_The_Impact_of_the_Outer_Coordination_Sphere_on_Electrocatalysts_for_Hydrogen_Production_and_Oxidation.pdf
2014-06-20 09:20:08, 4.27 M
» 收录本帖的淘帖专辑推荐
 Nano&Micro | 光催化专辑 | 氢能与电动汽车 | vasp |
| 催化相关 | 材料淘贴收录 | 感觉有用的帖子 |
» 猜你喜欢
修改论文，如何借助其他力量？
已经有4人回复
-
中山大学潘越教授课题组2027级推免硕士研究生招生 新增一个专业医学技术名额
已经有21人回复
-
金属材料论文润色/翻译怎么收费?
已经有54人回复
-
哈尔滨工程大学国家级青年人才-27年申请考核制博士招生（材料、化学、生物医学专业）
已经有12人回复
-
HRTEM/原位TEM/HRSTEM检测｜价格优·周期短·可加急
已经有0人回复
-
大家平时也可以交流下
已经有1人回复
» 本主题相关价值贴推荐，对您同样有帮助:
- Acc. Chem. Res上最新光催化综述：通过分子组装来提高光催化还原质子产氢效率
已经有92人回复
- 分享自己刚上线的AM：富缺陷二硫化钼超薄片用作产氢电催化剂
已经有130人回复
|
最新“干货”综述——Understanding TiO2 Photocatalysis: Mechanisms and Materials http://muchong.com/bbs/viewthread.php?tid=7924162 |
33楼2014-09-22 13:36:58
简单回复
2014-06-20 15:05
回复
五星好评 顶一下，感谢分享！
zxf9844楼
2014-06-20 15:06
回复
五星好评 顶一下，感谢分享！
2014-06-20 15:34
回复
五星好评 顶一下，感谢分享！
瑠可6楼
2014-06-20 16:26
回复
五星好评 顶一下，感谢分享！
8dianbao7楼
2014-06-21 10:09
回复
五星好评 顶一下，感谢分享！
马踏冰河8楼
2014-06-21 10:09
回复
五星好评 顶一下，感谢分享！
wjy20119楼
2014-06-21 10:29
回复
一般 顶一下，感谢分享！
fmbs11010楼
2014-06-21 16:59
回复
五星好评 顶一下，感谢分享！
delphoenix11楼
2014-06-22 22:53
回复
五星好评 顶一下，感谢分享！
xingkong9912楼
2014-06-23 01:45
回复
五星好评 顶一下，感谢分享！
never200413楼
2014-06-23 03:11
回复
五星好评 顶一下，感谢分享！
never200414楼
2014-06-23 03:11
回复
顶一下，感谢分享！
200