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相关概念视频

Oxidation of Phenols to Quinones01:17

Oxidation of Phenols to Quinones

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In the presence of oxidizing agents, phenols are oxidized to quinones. Quinones can be easily reduced back to phenols using mild reducing agents. The electron-donating hydroxyl group enhances the reactivity of the aromatic ring, enabling oxidation of the ring even in the absence of an α hydrogen.
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox...
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Radical Autoxidation01:20

Radical Autoxidation

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The oxidation of an organic compound in the presence of air or oxygen is called autoxidation. For example, cumene reacts with oxygen to form hydroperoxide. Autoxidation involves initiation, propagation, and termination steps. Many organic compounds are susceptible to autoxidation—especially ethers in the presence of oxygen, which form hydroperoxides. Even though this reaction is slow, old ether bottles contain small amounts of peroxide, which leads to laboratory explosions during ether...
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Redox Reactions01:27

Redox Reactions

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Redox reactions are vital biochemical processes that underpin energy metabolism in cells. These reactions involve the transfer of electrons between molecules, occurring in tandem as oxidation and reduction. Oxidation refers to the loss of electrons, while reduction denotes their gain. This coupling ensures the seamless flow of electrons through metabolic pathways. For example, in bacterial metabolism, glucose undergoes oxidation to carbon dioxide, while oxygen is simultaneously reduced to...
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Redox Reactions01:24

Redox Reactions

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Oxidation-reduction or redox reactions involve the transfer of electrons from one molecule or atom to another. When an atom gains an electron, another atom must lose an electron, meaning oxidation and reduction must occur together. Since the redox occurs in pairs, the atom that gets oxidized is also called the reducing agent or reductant, and the atom that is reduced is also called the oxidizing agent or oxidant. A straightforward way to remember the definitions of oxidation and reduction is...
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Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

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During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
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The Photochemical Reaction Center01:29

The Photochemical Reaction Center

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Reaction centers are pigment-protein complexes that initiate energy conversion from photons to chemical entities. Therefore, photochemical reaction center is a more appropriate term that describes these complexes. The Nobel laureates Robert Emerson and William Arnold provided the first experimental evidence of photochemical reaction centers by demonstrating the participation of nearly 2,500 chlorophyll molecules for the release of just one molecule of oxygen. Despite thousands of photosynthetic...
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这页已由机器翻译。其他页面可能仍然显示为英文。View in English
  1. 首页
  2. 研究领域
  3. 化学科学
  4. 有机化学
  5. 自由基化学
  6. 在flavoprotein Ferredoxin-nadp+活性位点中的光诱导,短寿命相互作用基的表征

在Flavoprotein Ferredoxin-NADP+活性位点中的光诱导,短寿命相互作用基的表征

Bo Zhuang1, Daisuke Seo2, Alexey Aleksandrov1

  • 1LOB, CNRS, INSERM, École Polytechnique, Institut Polytechnique de Paris, 91128 Palaiseau, France.

Journal of the American Chemical Society
|February 16, 2021

相关实验视频

Inactivation of Pathogens via Visible-Light Photolysis of Riboflavin-5′-Phosphate
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Inactivation of Pathogens via Visible-Light Photolysis of Riboflavin-5′-Phosphate

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Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
12:08

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry

Published on: March 18, 2012

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Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

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在PubMed 上查看摘要

概括
此摘要是机器生成的。

使用光谱学研究了黄蛋白中的超快电子转移. 研究人员对短寿命的中间激素进行了鉴定,

科学领域:

  • 生物化学
  • 光谱学
  • 酵素学

背景情况:

  • 黄胺二核酸 (FAD) 激素和氨基酸如氨酸和氨酸是黄蛋白电子转移 (ET) 反应中的关键中间体.
  • 在功能性黄蛋白过程中描述这些短寿命的中间体是具有挑战性的.
  • 由于FAD与氨酸 (Tyr50) 的相互作用,Bacillus subtilis中的ferredoxin-NADP+氧化还原酶 (BsFNR) 显示出强烈的光灭.

研究的目的:

  • 研究野生类型 (WT) BsFNR及其变体 (Tyr50被托或甘氨酸所取代) 的短寿命光产物.
  • 使用超快光谱方法在电荷分离状态下表征反应中间体.
  • 了解蛋白质环境和动态对基质中间体的光谱特性的影响.

主要方法:

  • 时间分辨率的光和吸收光谱.
  • 超快速光谱检测可光激活的黄蛋白.
  • 分子动力学模拟和量子力学计算.

主要成果:

  • 在WT BsFNR中,从Tyr50到激发的FAD辅因子的超快电子转移 (ET) 发生在260 fs左右.
  • 这种ET比电荷重组快得多,使电荷分离的中间体能够进行表征.
  • 对Y50W突变体的实验产生了与其他含酸的黄蛋白相似的光产物.

相关实验视频

Inactivation of Pathogens via Visible-Light Photolysis of Riboflavin-5′-Phosphate
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Inactivation of Pathogens via Visible-Light Photolysis of Riboflavin-5′-Phosphate

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Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
12:08

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry

Published on: March 18, 2012

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Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

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  • 离子基FAD的光谱特征对蛋白质环境和对电离子动态高度敏感.
  • 结论:

    • 参与黄蛋白功能过程的重要基质中间体的综合性表征.
    • 展示超快速ET作为一种促进中间特征的机制.
    • 突出了FAD激素的环境敏感性.