巯基弧菌醛氧化还原酶的直接电化学研究。

Margarida M Correia dos Santos, Patrícia M P Sousa, M Lurdes S Gonçalves, M João Romão, Isabel Moura, José J G Moura
{"title":"巯基弧菌醛氧化还原酶的直接电化学研究。","authors":"Margarida M Correia dos Santos,&nbsp;Patrícia M P Sousa,&nbsp;M Lurdes S Gonçalves,&nbsp;M João Romão,&nbsp;Isabel Moura,&nbsp;José J G Moura","doi":"10.1111/j.1432-1033.2004.04041.x","DOIUrl":null,"url":null,"abstract":"<p><p>This work reports on the direct electrochemistry of the Desulfovibrio gigas aldehyde oxidoreductase (DgAOR), a molybdenum enzyme of the xanthine oxidase family that contains three redox-active cofactors: two [2Fe-2S] centers and a molybdopterin cytosine dinucleotide cofactor. The voltammetric behavior of the enzyme was analyzed at gold and carbon (pyrolytic graphite and glassy carbon) electrodes. Two different strategies were used: one with the molecules confined to the electrode surface and a second with DgAOR in solution. In all of the cases studied, electron transfer took place, although different redox reactions were responsible for the voltammetric signal. From a thorough analysis of the voltammetric responses and the structural properties of the molecular surface of DgAOR, the redox reaction at the carbon electrodes could be assigned to the reduction of the more exposed iron cluster, [2Fe-2S] II, whereas reduction of the molybdopterin cofactor occurs at the gold electrode. Voltammetric results in the presence of aldehydes are also reported and discussed.</p>","PeriodicalId":11817,"journal":{"name":"European journal of biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2004-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1111/j.1432-1033.2004.04041.x","citationCount":"16","resultStr":"{\"title\":\"Direct electrochemistry of the Desulfovibrio gigas aldehyde oxidoreductase.\",\"authors\":\"Margarida M Correia dos Santos,&nbsp;Patrícia M P Sousa,&nbsp;M Lurdes S Gonçalves,&nbsp;M João Romão,&nbsp;Isabel Moura,&nbsp;José J G Moura\",\"doi\":\"10.1111/j.1432-1033.2004.04041.x\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>This work reports on the direct electrochemistry of the Desulfovibrio gigas aldehyde oxidoreductase (DgAOR), a molybdenum enzyme of the xanthine oxidase family that contains three redox-active cofactors: two [2Fe-2S] centers and a molybdopterin cytosine dinucleotide cofactor. The voltammetric behavior of the enzyme was analyzed at gold and carbon (pyrolytic graphite and glassy carbon) electrodes. Two different strategies were used: one with the molecules confined to the electrode surface and a second with DgAOR in solution. In all of the cases studied, electron transfer took place, although different redox reactions were responsible for the voltammetric signal. From a thorough analysis of the voltammetric responses and the structural properties of the molecular surface of DgAOR, the redox reaction at the carbon electrodes could be assigned to the reduction of the more exposed iron cluster, [2Fe-2S] II, whereas reduction of the molybdopterin cofactor occurs at the gold electrode. Voltammetric results in the presence of aldehydes are also reported and discussed.</p>\",\"PeriodicalId\":11817,\"journal\":{\"name\":\"European journal of biochemistry\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2004-04-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1111/j.1432-1033.2004.04041.x\",\"citationCount\":\"16\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"European journal of biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1111/j.1432-1033.2004.04041.x\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"European journal of biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1111/j.1432-1033.2004.04041.x","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 16

摘要

本文报道了DgAOR (Desulfovibrio gigas aldehyde oxidoreductase, DgAOR)的直接电化学反应,DgAOR是黄嘌呤氧化酶家族中的一种钼酶,含有三个氧化还原活性辅助因子:两个[2Fe-2S]中心和一个钼胞嘧啶二核苷酸辅助因子。在金和碳(热解石墨和玻璃碳)电极上分析了酶的伏安行为。使用了两种不同的策略:一种是将分子限制在电极表面,另一种是在溶液中使用DgAOR。在所有研究的情况下,电子转移发生了,尽管不同的氧化还原反应负责伏安信号。通过对DgAOR分子表面的伏安响应和结构特性的深入分析,碳电极上的氧化还原反应可以归因于更多暴露的铁簇[2Fe-2S] II的还原,而钼酸盐辅因子的还原发生在金电极上。在醛的存在伏安结果也被报道和讨论。
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
Direct electrochemistry of the Desulfovibrio gigas aldehyde oxidoreductase.

This work reports on the direct electrochemistry of the Desulfovibrio gigas aldehyde oxidoreductase (DgAOR), a molybdenum enzyme of the xanthine oxidase family that contains three redox-active cofactors: two [2Fe-2S] centers and a molybdopterin cytosine dinucleotide cofactor. The voltammetric behavior of the enzyme was analyzed at gold and carbon (pyrolytic graphite and glassy carbon) electrodes. Two different strategies were used: one with the molecules confined to the electrode surface and a second with DgAOR in solution. In all of the cases studied, electron transfer took place, although different redox reactions were responsible for the voltammetric signal. From a thorough analysis of the voltammetric responses and the structural properties of the molecular surface of DgAOR, the redox reaction at the carbon electrodes could be assigned to the reduction of the more exposed iron cluster, [2Fe-2S] II, whereas reduction of the molybdopterin cofactor occurs at the gold electrode. Voltammetric results in the presence of aldehydes are also reported and 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
自引率
0.00%
发文量
0
期刊最新文献
The citation of bibliographic references in biochemical journals. Recommendations 1971. Carbamoylphosphate synthetase from Pseudomonas aeruginosa. Subunit composition, kinetic analysis and regulation. Nuclear magnetic resonance of protamines. A 13C relaxation study of the three main fractions of clupeine. Stereochemistry of the hydrolysis of trehalose by the enzyme trehalase prepared from the flesh fly Sarcophaga barbata. Studies on energy supply for genetic processes. Requirement for membrane potential in Escherichia coli infection by phage T4.
×
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