Elucidating mechanisms of biological hydrogen conversion through model metalloenzymes
通过模型金属酶阐明生物氢转化机制
基本信息
- 批准号:2419343
- 负责人:
- 金额:$ 42.9万
- 依托单位:
- 依托单位国家:美国
- 项目类别:Standard Grant
- 财政年份:2024
- 资助国家:美国
- 起止时间:2024-04-01 至 2024-09-30
- 项目状态:已结题
- 来源:
- 关键词:
项目摘要
With the support of the Chemistry of Life Processes Program in the Chemistry Division, Professor Hannah Shafaat of The Ohio State University will investigate the factors that govern the activity of nickel-containing enzymes. Reductive nickel enzymes are critical in the metabolic processes of diverse microorganisms and perform valuable reactions such as hydrogen production, carbon dioxide reduction, and methane oxidation. These efficient, complex enzymes operate with high rates and full reversibility but have yet to be accurately reproduced in synthetic systems, leaving many questions unanswered. To better understand native nickel enzymes and learn how to harness this understanding for anthropogenic processes, the Shafaat group will model the nickel-iron hydrogenases using a robust, protein-based scaffold. The proposed studies on the engineered enzymes are aimed at the elucidation of the reaction mechanisms along with the identification of the key factors along the entire protein contributing to catalysis. The research provides insight into how natural enzymes function across a range of length- and timescales. Graduate, undergraduate, and high-school students, including those from underserved communities, will be trained in state-of-the-art research techniques spanning biological, inorganic, physical, and analytical chemistry. This award also supports the development of lectures and hands-on exercises to train members of the broader bioinorganic community who attend the internationally recognized, biennial Penn State Bioinorganic Workshop. This project will be integrated with outreach programs spanning multiple age groups in greater Central Ohio. This project seeks to address critical knowledge gaps about the naturally occurring nickel-iron hydrogenases and related nickel-thiolate enzymes through the development and characterization of a model hydrogenase enzyme, namely nickel-substituted rubredoxin (NiRd). Prior work supported by the NSF in the Shafaat group has established that NiRd is a functional mimic of hydrogenase that exhibits high rates for hydrogen evolution. In the proposed work, spectroscopic techniques, including electron paramagnetic resonance, nuclear magnetic resonance, resonance Raman, and X-ray absorption, coupled with electrochemical methods, will be employed to obtain high-resolution mechanistic information and to reveal molecular-level contributors to hydrogen evolution activity. These studies will provide detailed insight into the layers of control exerted by the protein scaffold in both model and native metalloenzymes. The goals of the work are to identify correlations between enzymatic structure and function and to advance our understanding of biological hydrogen conversion. The research seeks also to identify design principles for highly active artificial metalloenzymes, with long-term implications for the development of sustainable catalysts for small molecule activation reactions.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.
在化学系生命过程化学项目的支持下,俄亥俄州州立大学的Hannah Shafaat教授将研究控制含镍酶活性的因素。还原性镍酶在多种微生物的代谢过程中至关重要,并进行有价值的反应,如制氢,二氧化碳还原和甲烷氧化。这些高效、复杂的酶以高速率和完全可逆性运行,但尚未在合成系统中准确复制,留下许多问题没有答案。为了更好地了解天然镍酶,并学习如何利用这种理解人为过程,Shafaat小组将使用一种强大的基于蛋白质的支架来模拟镍铁氢化酶。对工程化酶的拟议研究旨在阐明反应机制,沿着鉴定有助于催化的整个蛋白质的关键因子沿着。这项研究提供了对天然酶如何在一系列长度和时间尺度上发挥作用的深入了解。研究生,本科生和高中生,包括来自服务不足社区的学生,将接受跨越生物,无机,物理和分析化学的最先进研究技术的培训。该奖项还支持讲座和实践练习的发展,以培训参加国际公认的两年一度的宾夕法尼亚州立大学生物无机研讨会的更广泛的生物无机社区的成员。该项目将与跨越俄亥俄州中部多个年龄组的外展计划相结合。该项目旨在通过开发和表征一种模型氢化酶,即镍取代的rubredoxin(NiRd),来解决有关天然存在的镍铁氢化酶和相关镍硫醇化酶的关键知识缺口。由NSF支持的Shafaat小组的先前工作已经确定NiRd是氢化酶的功能模拟物,其表现出高的析氢速率。在拟议的工作中,光谱技术,包括电子顺磁共振,核磁共振,共振拉曼,和X-射线吸收,加上电化学方法,将被用来获得高分辨率的机制信息,并揭示分子水平的贡献者析氢活动。 这些研究将提供详细的洞察层的控制所施加的蛋白质支架模型和天然金属酶。 这项工作的目标是确定酶结构和功能之间的相关性,并促进我们对生物氢转化的理解。 该研究还旨在确定高活性人工金属酶的设计原则,对小分子活化反应的可持续催化剂的开发具有长期影响。该奖项反映了NSF的法定使命,并通过使用基金会的知识价值和更广泛的影响审查标准进行评估,被认为值得支持。
项目成果
期刊论文数量(0)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
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Hannah Shafaat其他文献
Hannah Shafaat的其他文献
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{{ truncateString('Hannah Shafaat', 18)}}的其他基金
NSF-DFG EChem: CAS: Mechanistic Interrogation of Electrocatalytic Hydrogen Evolution by an Artificial Hydrogenase
NSF-DFG EChem:CAS:人工氢化酶电催化析氢的机械询问
- 批准号:
2346885 - 财政年份:2023
- 资助金额:
$ 42.9万 - 项目类别:
Standard Grant
Elucidating mechanisms of biological hydrogen conversion through model metalloenzymes
通过模型金属酶阐明生物氢转化机制
- 批准号:
2108684 - 财政年份:2021
- 资助金额:
$ 42.9万 - 项目类别:
Standard Grant
NSF-DFG EChem: CAS: Mechanistic Interrogation of Electrocatalytic Hydrogen Evolution by an Artificial Hydrogenase
NSF-DFG EChem:CAS:人工氢化酶电催化析氢的机械询问
- 批准号:
2140211 - 财政年份:2021
- 资助金额:
$ 42.9万 - 项目类别:
Standard Grant
CAREER: Metalloenzyme mechanisms probed by resonance Raman spectroscopy
职业:通过共振拉曼光谱探测金属酶机制
- 批准号:
1454289 - 财政年份:2015
- 资助金额:
$ 42.9万 - 项目类别:
Continuing Grant
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