Jove
Visualize
联系我们
JoVE
x logofacebook logolinkedin logoyoutube logo
关于 JoVE
概览领导团队博客JoVE 帮助中心
作者
出版流程编辑委员会范围与政策同行评审常见问题投稿
图书馆员
用户评价订阅访问资源图书馆顾问委员会常见问题
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experiments存档
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教师资源中心教师网站
使用条款与条件
隐私政策
政策

相关概念视频

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)01:20

¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)

1.0K
When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
1.0K
IR Frequency Region: Fingerprint Region01:03

IR Frequency Region: Fingerprint Region

798
IR spectra are divided into two main regions: the diagnostic region and the fingerprint region. The diagnostic region of the spectrum lies above 1500 cm−1. The absorptions resulting from single-bond vibrations of the N–H, C–H, and O–H stretch at higher wavenumbers and appear on the left side of the spectrum. The stretching absorptions of the C≡C and C≡N occur between 2100–2300 cm−1. In contrast, those arising from stretching absorptions of the...
798
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

2.1K
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
2.1K
IR Frequency Region: X–H Stretching01:24

IR Frequency Region: X–H Stretching

925
In IR spectroscopy, signals produced by the X−H bonds (such as C−H, O−H, or N−H) can be observed in the frequency range of  2700–4000 cm–1. The C−H stretching vibration forms sharp bands in the region 2850–3000 cm–1. The presence of the O−H stretching vibration leads to the forming of an absorption band in the frequency range 3650–3200 cm−1. At the same time, N−H stretching can be confirmed by absorption bands in...
925
Infrared (IR) Spectroscopy: Overview01:09

Infrared (IR) Spectroscopy: Overview

1.5K
When electromagnetic radiation passes through a material, atoms or molecules transition from a lower to a higher energy state by absorbing radiation corresponding to the energy difference between the two states. The absorption of infrared (IR) radiation causes transitions between vibrational energy levels in a molecule. Therefore, IR spectroscopy is a useful analytical tool for determining the molecular structure of molecules.
Different compounds display unique properties due to their...
1.5K

您也可能阅读

相关文章

通过共同作者、期刊和引用图与本文相关的文章。

排序
Same author

Architecture of the 8 MDa Hdr-Vhu-Fwd super-assembly in class I methanogens.

Nature·2026
Same author

Stereocontrol as a tool for shaping abiotic, sequence-defined oligourethanes.

Polymer chemistry·2026
Same author

Direct Electrochemistry of Hydrogenase, Formate Dehydrogenase, CO Dehydrogenase, and Nitrogenase: Wiring Strategies and Mechanistic Insights into Metalloenzymes That Produce Solar Fuels.

Chemical reviews·2026
Same author

Structural basis of membrane potential coupled vectorial CO₂ hydration by the DAB2 complex in chemolithoautotrophs.

Nature communications·2026
Same author

Interfacing Broad-Spectrum Semiconductors with Hydrogenases for Semi-Artificial Solar Reforming of Cellulose.

Journal of the American Chemical Society·2026
Same author

A Zundel ion in the catalytic proton transfer pathway of [FeFe]-hydrogenase.

Physical chemistry chemical physics : PCCP·2026

相关实验视频

Updated: Jun 13, 2025

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

12.2K

通过红外差异光谱学探测铁素:酶电子转移复合体.

Selmihan Sahin1,2, Johanna Brazard3, Kilian Zuchan1

  • 1University of Geneva, Department of Inorganic and Analytical Chemistry, Sciences II Quai Ernest-Ansermet 30 Geneva 4 1211 Switzerland ross.milton@unige.ch.

Chemical science
|May 14, 2025
PubMed
概括

铁素通过连续的单电子转移促进多电子氧化还原反应. 这项研究揭示了铁素和基酶如何相互作用,使生物过程能够有效地转移电子.

更多相关视频

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

17.9K
Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
12:07

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry

Published on: March 24, 2012

16.2K

相关实验视频

Last Updated: Jun 13, 2025

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

12.2K
Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

17.9K
Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry
12:07

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry

Published on: March 24, 2012

16.2K

科学领域:

  • 生物化学 生物化学
  • 生物能源学 生物能源学
  • 蛋白质与蛋白质的相互作用

背景情况:

  • 铁素是生物氧化还原反应中至关重要的电子载体.
  • 铁素促进多电子转移的机制尚不清楚.
  • 了解这些机制对于光合作用和代谢等领域至关重要.

研究的目的:

  • 为了研究密闭铁素 (CpFd) 和[FeFe]-基酶之间的电子转移复合体.
  • 阐明铁素结构和氧化还原状态在调节蛋白-蛋白相互作用 (PPI) 中的作用.
  • 提出一种由铁素介导的高效多电子转移模型.

主要方法:

  • 使用富里埃变换红外光谱 (FTIR) 和非正规氨基酸探测电场变化.
  • 在现场使用FTIR差异光谱来观察减少后的蛋白质结构变化.
  • 应用微尺度热泳以量化铁素酶结合亲缘关系.

主要成果:

  • 在CpFd中引入了一种非正规的氨基酸,通过振动Stark效应量化电场变化.
  • 在铁素和酶之间观察到蛋白质结构变化和量化氧化还原依赖PPI.
  • 证明了铁素-酶亲和力是由铁素的氧化还原状态调节的.

结论:

  • 铁素通过一系列单电子转移事件促进多电子还氧化化学.
  • 红氧依赖PPI在电子转移的效率中起着至关重要的作用.
  • 这些发现为铁素介导的多电子转移提供了一个机制模型.