EPR spectroscopy of putative enzyme intermediates in the NO reductase and the auto‐nitrosylation reaction of Desulfovibrio vulgaris Desulfovibrio vulgaris hybrid cluster protein

Hagen Wilfred R.

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EPR spectroscopy of putative enzyme intermediates in the NO reductase and the auto‐nitrosylation reaction of Desulfovibrio vulgaris Desulfovibrio vulgaris hybrid cluster protein

机译：预备酶中间体的EPR光谱法中间体中间体和脱硫脱硫蛋白脱硫脱硫簇蛋白的脱硫脱硫蛋白的自硝基化反应

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The hybrid cluster protein (Hcp) contains a unique 4Fe cluster that is a hybrid of μ‐S and μ‐O bridges. Escherichia?coli Hcp has recently been found to carry NO reductase activity as well as S ‐nitrosylation activity in NO‐based signaling. In other species, the physiological activity has not been established. No reaction mechanism of any Hcp has been proposed. Here, we show that Desulfovibrio?vulgaris (Hildenborough) Hcp has nitric oxide reductase activity with benzyl viologen as electron donor. With EPR spectroscopy, we identify three unexpected putative reaction intermediates: both in reduced and oxidized Hcp, dinitrosyl iron complexes are formed. Also, the hybrid cluster in reduced Hcp, but not in oxidized Hcp, binds the product N 2 O. Possible implications for a reaction mechanism are discussed.

机译：杂交簇蛋白（HCP）包含独特的4FE簇，其是μ-S和μ-O桥的混合。大肠杆菌？最近发现Coli HCP在无基信号中无携带还原酶活性以及S-腈化活性。在其他物种中，尚未建立生理活动。没有提出任何HCP的反应机制。在这里，我们展示了Desulfovirio？寻常（Hildenborough）HCP与苄基Viologen作为电子给体具有一氧化氮还原酶活性。利用EPR光谱学，我们鉴定了三种意外推定的反应中间体：在减少和氧化HCP中，形成二硝基铁复合物。此外，还原HCP中的杂交簇，但不在氧化HCP中结合产物N 2 O.讨论了对反应机制的可能影响。

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《FEBS letters.》 |2019年第21期|共9页
作者
Hagen Wilfred R.;
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作者单位

Department of BiotechnologyDelft University of TechnologyDelft the Netherlands;

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正文语种 eng
中图分类生物化学;
关键词
Desulfovibrio; EPR; hybrid cluster protein; nitric oxide; nitrosylation; NO reductase;

机译：Desulfovibrio;epr;杂交簇蛋白;一氧化氮;亚硝基化;没有还原酶;

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2. EPR spectroscopy of putative enzyme intermediates in the NO reductase and the auto‐nitrosylation reaction of Desulfovibrio vulgaris Desulfovibrio vulgaris hybrid cluster protein [J] . Hagen Wilfred R. FEBS letters. . 2019,第21期

机译：预备酶中间体的EPR光谱法中间体中间体和脱硫脱硫蛋白脱硫脱硫簇蛋白的脱硫脱硫蛋白的自硝基化反应
3. Reduced hybrid cluster proteins (HCP) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at high resolution using synchrotron radiation [J] . David Aragao, Sofia Macedo, Edward P. Mitchell, Journal of biological inorganic chemistry: JBIC: a publication of the Society of Biological Inorganic Chemistry . 2003,第5期

机译：脱硫脱硫弧菌ATCC 27774和寻常脱硫弧菌（希尔登伯勒）的杂化簇蛋白（HCP）减少：使用同步加速器辐射以高分辨率显示X射线结构
4. Hybrid cluster proteins (HCPs) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at 1.25 A resolution using synchrotron radiation [J] . Sofia Macedo, Edward P. Mitchell, Celia V. Romao, Journal of biological inorganic chemistry: JBIC: a publication of the Society of Biological Inorganic Chemistry . 2002,第4a5期

机译：来自脱硫脱硫弧菌ATCC 27774和寻常脱硫弧菌（希尔登伯勒）的杂种簇蛋白（HCP）：使用同步加速器辐射以1.25 A的分辨率解析X射线结构
5. Analysis of Intact Sulfite Reductase, Dissimilatory Form, Protein Complex from Desulfovibrio vulgaris Using Ion Mobility QTOF Analyzer [C] . Ming Dong, Michael Daly, Haichuan Liu, ASMS Conference on Mass Spectrometry and Allied Topics . 2008

机译：采用离子迁移率QTOF分析仪从脱硫术中完整亚硫酸盐还原酶，散发形式，蛋白质复合物的分析
6. Part 1. The role of nickel in carcinogenesis, methanogenesis and transcriptional regulation. Part 2. An X-ray absorption study of Desulfovibrio vulgaris superoxide reductase. [D] . Carrington, Paul Edward. 2003

机译：第1部分。镍在癌变，甲烷生成和转录调控中的作用。第2部分。寻常脱硫弧菌超氧化物还原酶的X射线吸收研究。
7. Hybrid Cluster Proteins and Flavodiiron Proteins Afford Protection to Desulfovibrio vulgaris upon Macrophage Infection [O] . Mafalda C. O. Figueiredo, Susana A. L. Lobo, Sara H. Sousa, 2013

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8. Multi-frequency EPR and high-resolution MÖssbauer spectroscopy of a putative [6Fe-6S] prismane-cluster-containing protein from Desulfovibrio vulgaris (Hildenborough) [O] . Pierik, Antonio J., Hagen, Wilfred R., Dunham, W. Richard, 1992

机译：来自Desulfovibrio vulgaris（Hildenborough）的推定的[6Fe-6s]含有人类簇蛋白的多频EpR和高分辨率mÖssbauer光谱

EPR spectroscopy of putative enzyme intermediates in the NO reductase and the auto‐nitrosylation reaction of Desulfovibrio vulgaris Desulfovibrio vulgaris hybrid cluster protein

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