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Ligand Binding and Linkage00:49

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
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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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Color in Coordination Complexes
When atoms or molecules absorb light at the proper frequency, their electrons are excited to higher-energy orbitals. For many main group atoms and molecules, the absorbed photons are in the ultraviolet range of the electromagnetic spectrum, which cannot be detected by the human eye. For coordination compounds, the energy difference between the d orbitals often allows photons in the visible range to be absorbed and emitted, which is seen as colors by the human...
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Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides
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对超氧化物脱酶动态中的铜结合的多模式反应.

Marta Bonaccorsi1, Michael J Knight1, Tanguy Le Marchand1

  • 1Centre de RMN à Très Hauts Champs, FRE 2034 (CNRS/Université Claude Bernard Lyon 1/Ecole Normale Supérieure de Lyon), University of Lyon, 69100 Villeurbanne, France.

Journal of the American Chemical Society
|November 9, 2020
PubMed
概括

铜/超氧化物脱酶 (SOD) 的动态被研究在两个金属化形式. 金属离子的吸收调节了蛋白质的灵活性,影响了各种时间尺度上的运动.

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科学领域:

  • 生物化学 生物化学
  • 生物物理学的生物物理.
  • 结构生物学 结构生物学

背景情况:

  • 铜/超氧化物脱酶 (SOD) 是一种关键的金属酶,与肌缩性侧面硬化症有关.
  • 了解SOD的结构功能关系对于神经退行性疾病研究至关重要.

研究的目的:

  • 为了研究金属化对SOD动态的影响.
  • 在SOD的不同金属化状态下量化蛋白质运动.

主要方法:

  • 固态核磁共振 (NMR) 光谱学. 固态核磁共振 (NMR) 光谱学.
  • 在高磁场 (800-1000 MHz) 中,快速的魔法角旋转 (MAS).
  • 对Cu,Zn-SOD和E,Zn-SOD的微晶制剂的分析.

主要成果:

  • 金属离子吸收不会使SOD变硬,而是重新分配运动过程.
  • 运动被量化在一个从纳秒到毫秒的动态范围.
  • 观察到histidine侧链动态和远程骨干元素之间的合.

结论:

  • 金属化状态显著影响SOD的动态景观.
  • 由于金属离子的结合,SOD的灵活性受到微调,影响蛋白质的功能.
  • 这些发现提供了关于SOD在疾病机制中的作用的见解.