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相关概念视频

Induced-fit Model01:13

Induced-fit Model

Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical characteristics of...
Reaction Mechanisms03:06

Reaction Mechanisms

Chemical reactions often occur in a stepwise fashion, involving two or more distinct reactions taking place in a sequence. A balanced equation indicates the reacting species and the product species, but it reveals no details about how the reaction occurs at the molecular level. The reaction mechanism (or reaction path) provides details regarding the precise, step-by-step process by which a reaction occurs.
For instance, the decomposition of ozone appears to follow a mechanism with two steps:
Catalysis02:50

Catalysis

The presence of a catalyst affects the rate of a chemical reaction. A catalyst is a substance that can increase the reaction rate without being consumed during the process. A basic comprehension of a catalysts’ role during chemical reactions can be understood from the concept of reaction mechanisms and energy diagrams.
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
Catalysis01:27

Catalysis

Catalysis influences the rate of chemical reactions by providing an alternative reaction pathway with lower activation energy. A catalyst speeds up a reaction, but it is not consumed during the process. The fundamental principle of catalysis is the ability of a catalyst to alter the reaction mechanism, often introducing a more efficient pathway than the uncatalyzed process.In a catalyzed reaction, the catalyst participates directly in the reaction mechanism. It interacts with reactants to form...

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相关实验视频

Updated: Jul 5, 2026

Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry
09:14

Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry

Published on: July 20, 2016

一个量子化学研究的反应机制的乙-辅酶合成酶.

Patricia Amara1, Anne Volbeda, Juan Carlos Fontecilla-Camps

  • 1Laboratoire de Dynamique Moléculaire and Laboratoire de Cristallographie et Cristallogenèse des Protéines, Institut de Biologie Structurale - Jean-Pierre Ebel, CEA/CNRS/UJF, 41, rue Jules Horowitz, F-38027 Grenoble Cedex 01, France.

Journal of the American Chemical Society
|February 24, 2005
PubMed
概括

这项研究调查了乙-CoA合成酶的活性部位,该研究显示,单核机制受到青,封闭形式必须打开以适应连接体. 还讨论了氧化还原状态和二硫化物键形成.

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08:34

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Last Updated: Jul 5, 2026

Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry
09:14

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Published on: July 20, 2016

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科学领域:

  • 生物化学 生物化学
  • 计算化学计算化学
  • 酶的机制 酶的机制

背景情况:

  • 乙-CoA合成酶 (ACS) 从甲基,CO和CoA中催化乙-CoA的合成.
  • 目前正在研究A集群活性位点的机制,特别是其金属中心的氧化还原状态.
  • 关于 (Ni-Ni) 双金属中心和铁硫团的作用,有几项建议存在.

研究的目的:

  • 为了研究乙-CoA合成酶的催化循环中的假定中间状态.
  • 阐明在A集群活性部位的乙-CoA合成机制.
  • 为了澄清活性部位内的氧化还原状态和配体结合.

主要方法:

  • 使用混合密度函数理论 (DFT) 的计算.
  • 在催化循环中研究各种中间状态.
  • 对拟议的反应机制和氧化还原状态的分析.

主要成果:

  • 接近金属的零价值状态不太可能与+2铁硫集束电荷.
  • 一个单核机制,其中CO和CH3都与近接结合,比一个双核机制更受青.
  • 如果甲基化同时进行,二硫化键的形成可以提供必要的电子.
  • 活性位点的结晶学封闭形式必须为赤道连接体的容纳开放.

结论:

  • 单核机制是ACS.通过乙-CoA合成的首选.
  • 特定的氧化还原状态和结构结构对酶功能至关重要.
  • 了解这些机制细节可以了解生物碳固定和能量转化.