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

Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

9.7K
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...
9.7K
Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

19.6K
The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
19.6K
The Supercomplexes in the Crista Membrane01:41

The Supercomplexes in the Crista Membrane

3.2K
The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
3.2K
Electron Transport Chains01:28

Electron Transport Chains

117.3K
The final stage of cellular respiration is oxidative phosphorylation that consists of two steps: the electron transport chain and chemiosmosis. The electron transport chain is a set of proteins found in the inner mitochondrial membrane in eukaryotic cells. Its primary function is to establish a proton gradient that can be used during chemiosmosis to produce ATP and generate electron carriers, such as NAD+ and FAD, that are used in glycolysis and the citric acid cycle.
The ETC is comprised of...
117.3K
Gene Families01:57

Gene Families

10.2K
Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
10.2K
Pyruvate Oxidation01:15

Pyruvate Oxidation

172.1K
After glycolysis, the charged pyruvate molecules enter the mitochondria via active transport and undergo three enzymatic reactions. These reactions ensure that pyruvate can enter the next metabolic pathway so that energy stored in the pyruvate molecules can be harnessed by the cells.
First, the enzyme pyruvate dehydrogenase removes the carboxyl group from pyruvate and releases it as carbon dioxide. The stripped molecule is then oxidized and releases electrons, which are then picked up by NAD+...
172.1K

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

A closely related pair of superoxide dismutase isozymes from Staphylococcus aureus show distinct stabilities and proton-exchange dynamics.

The Journal of biological chemistry·2026
Same author

Structural insights into cobalamin loading and reactivation of human methionine synthase.

Nature communications·2026
Same author

Structural basis of iron piracy by human gut <i>Bacteroides</i>.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

BtuJ1, a Surface-exposed B<sub>12</sub>-binding Protein in Bacteroidota, Functions as an Extracellular Vitamin Reservoir That Enhances Fitness.

Journal of molecular biology·2026
Same author

Copper requirements and copper toxicity as niche-defining factors in the growth of terrestrial ammonia-oxidizing archaea and bacteria.

FEMS microbiology ecology·2026
Same author

Hydrazine Synthase From Anammox Is Inhibited by Linear and Aromatic Alkynes.

Environmental microbiology·2026

相关实验视频

Updated: Apr 5, 2026

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

10.0K

一个四螺旋束储存铜用于甲氧化

Nicolas Vita1, Semeli Platsaki1, Arnaud Baslé1

  • 1Institute for Cell and Molecular Biosciences, Medical School, Newcastle University, Newcastle upon Tyne NE2 4HH, UK.

Nature
|August 27, 2015
PubMed
概括

研究人员在甲氧化细菌中发现了一种新型的储铜蛋白 (Csp1). 这种蛋白质对于储存甲氧化所需的铜至关重要,这是控制温室气体和生物技术应用的重要过程.

更多相关视频

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

10.2K
Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
05:27

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

Published on: July 20, 2022

2.3K

相关实验视频

Last Updated: Apr 5, 2026

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
11:04

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

10.0K
Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

10.2K
Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
05:27

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools

Published on: July 20, 2022

2.3K

科学领域:

  • 生物化学
  • 微生物学
  • 环境科学

背景情况:

  • 甲氧化细菌 (甲营养菌) 使用依赖铜的甲单氧酶进行甲氧化.
  • 甲单氧酶是大气中的甲调节的关键,
  • 甲类植物在生物修复,化学合成和生物能源方面具有显著的潜力.

研究的目的:

  • 在*Methylosinus trichosporium* OB3b中发现和描述一种新的铜储存蛋白.
  • 阐明甲中甲氧化的铜储存机制.
  • 了解铜储存在甲类植物中的生物技术含义.

主要方法:

  • 新型铜储蛋白 (Csp1) 的分离和表征
  • Csp1的结构分析,包括它的四级结构和铜结合点.
  • 对Csp1在甲单氧酶活性中的铜恒温作用的研究.

主要成果:

  • 在*Methylosinus trichosporium* OB3b中发现出口的铜储存蛋白Csp1.
  • Csp1是一种具有独特的铜结合机制的四聚体,涉及氨酸残留物.
  • 在已知的蛋白质折叠模式中储存铜,这是金属储存蛋白质的新发现.
  • 在多种细菌中识别细胞质Csp1同类,挑战以前关于铜使用的假设.

结论:

  • Csp1在甲类动物中对颗粒甲单氧酶的铜积累起着至关重要的作用.
  • Csp1的独特结构和功能为细菌中的铜代谢提供了关键的见解.
  • 了解Csp1对于充分利用甲类植物的生物技术潜力至关重要.