甲酸脱氢酶:从NAD(P)H再生到靶向病原体生物膜,组成高效杂交生物催化剂和大气CO2固定

IF 0.7 Q4 CHEMISTRY, MULTIDISCIPLINARY
V. I. Tishkov, A. A. Pometun, S. S. Savin
{"title":"甲酸脱氢酶:从NAD(P)H再生到靶向病原体生物膜,组成高效杂交生物催化剂和大气CO2固定","authors":"V. I. Tishkov,&nbsp;A. A. Pometun,&nbsp;S. S. Savin","doi":"10.3103/S0027131423040077","DOIUrl":null,"url":null,"abstract":"<p>NAD(P)<sup>+</sup>-dependent formate dehydrogenase (EC 1.2.1.2, FDH) catalyzes the simplest reaction from chemical and biological points of view, oxidation of formate-ion to carbon dioxide coupled to NAD(P)<sup>+</sup> reduction to yield NAD(P)H. Advances in the life sciences have shown that this reaction plays an extremely important role in a wide variety of organisms. The areas and types of practical applications of FDH are also permanently expanding. The review analyzes the key steps in the development of our knowledge on the role of formate dehydrogenase in living systems. Achievements in creation of highly efficient catalysts based on FDH for classic biotechnology as well as for new areas are also considered. The importance of a correct selection of the starting FDH form for the purpose of a biocatalyst design with required properties with minimal costs is demonstrated. The prospects for the use of FDH for CO<sub>2</sub> fixation of CO<sub>2</sub> are discussed.</p>","PeriodicalId":709,"journal":{"name":"Moscow University Chemistry Bulletin","volume":"78 4","pages":"151 - 169"},"PeriodicalIF":0.7000,"publicationDate":"2023-08-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":"{\"title\":\"Formate Dehydrogenase: From NAD(P)H Regeneration to Targeting Pathogen Biofilms, Composing Highly Efficient Hybrid Biocatalysts and Atmospheric CO2 Fixation\",\"authors\":\"V. I. Tishkov,&nbsp;A. A. Pometun,&nbsp;S. S. Savin\",\"doi\":\"10.3103/S0027131423040077\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>NAD(P)<sup>+</sup>-dependent formate dehydrogenase (EC 1.2.1.2, FDH) catalyzes the simplest reaction from chemical and biological points of view, oxidation of formate-ion to carbon dioxide coupled to NAD(P)<sup>+</sup> reduction to yield NAD(P)H. Advances in the life sciences have shown that this reaction plays an extremely important role in a wide variety of organisms. The areas and types of practical applications of FDH are also permanently expanding. The review analyzes the key steps in the development of our knowledge on the role of formate dehydrogenase in living systems. Achievements in creation of highly efficient catalysts based on FDH for classic biotechnology as well as for new areas are also considered. The importance of a correct selection of the starting FDH form for the purpose of a biocatalyst design with required properties with minimal costs is demonstrated. The prospects for the use of FDH for CO<sub>2</sub> fixation of CO<sub>2</sub> are discussed.</p>\",\"PeriodicalId\":709,\"journal\":{\"name\":\"Moscow University Chemistry Bulletin\",\"volume\":\"78 4\",\"pages\":\"151 - 169\"},\"PeriodicalIF\":0.7000,\"publicationDate\":\"2023-08-17\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Moscow University Chemistry Bulletin\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://link.springer.com/article/10.3103/S0027131423040077\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"CHEMISTRY, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Moscow University Chemistry Bulletin","FirstCategoryId":"1085","ListUrlMain":"https://link.springer.com/article/10.3103/S0027131423040077","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
引用次数: 1

摘要

NAD(P)+依赖的甲酸脱氢酶(EC 1.2.1.2, FDH)催化的反应从化学和生物学角度看都是最简单的,甲酸离子氧化生成二氧化碳,再结合NAD(P)+还原生成NAD(P)H。生命科学的进步表明,这种反应在各种各样的生物体中起着极其重要的作用。外佣的实际应用领域和类型也在不断扩大。本文分析了甲酸脱氢酶在生命系统中作用的研究进展的关键步骤。在经典生物技术和新领域中,基于FDH的高效催化剂的创造也得到了考虑。本文论证了正确选择起始外佣形式对于设计具有所需性能和最低成本的生物催化剂的重要性。讨论了利用FDH固CO2的前景。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Formate Dehydrogenase: From NAD(P)H Regeneration to Targeting Pathogen Biofilms, Composing Highly Efficient Hybrid Biocatalysts and Atmospheric CO2 Fixation

Formate Dehydrogenase: From NAD(P)H Regeneration to Targeting Pathogen Biofilms, Composing Highly Efficient Hybrid Biocatalysts and Atmospheric CO2 Fixation

NAD(P)+-dependent formate dehydrogenase (EC 1.2.1.2, FDH) catalyzes the simplest reaction from chemical and biological points of view, oxidation of formate-ion to carbon dioxide coupled to NAD(P)+ reduction to yield NAD(P)H. Advances in the life sciences have shown that this reaction plays an extremely important role in a wide variety of organisms. The areas and types of practical applications of FDH are also permanently expanding. The review analyzes the key steps in the development of our knowledge on the role of formate dehydrogenase in living systems. Achievements in creation of highly efficient catalysts based on FDH for classic biotechnology as well as for new areas are also considered. The importance of a correct selection of the starting FDH form for the purpose of a biocatalyst design with required properties with minimal costs is demonstrated. The prospects for the use of FDH for CO2 fixation of CO2 are discussed.

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
Moscow University Chemistry Bulletin
Moscow University Chemistry Bulletin CHEMISTRY, MULTIDISCIPLINARY-
CiteScore
1.30
自引率
14.30%
发文量
38
期刊介绍: Moscow University Chemistry Bulletin is a journal that publishes review articles, original research articles, and short communications on various areas of basic and applied research in chemistry, including medical chemistry and pharmacology.
×
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
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
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 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信