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Related Concept Videos

Acid-Catalyzed Dehydration of Alcohols to Alkenes02:35

Acid-Catalyzed Dehydration of Alcohols to Alkenes

In a dehydration reaction, a hydroxyl group in an alcohol is eliminated along with the hydrogen from an adjacent carbon. Here, the products are an alkene and a molecule of water. Dehydration of alcohols is generally achieved by heating in the presence of an acid catalyst. While the dehydration of primary alcohols requires high temperatures and acid concentrations, secondary and tertiary alcohols can lose a water molecule under relatively mild conditions.
Preparation of Alcohols via Addition Reactions02:15

Preparation of Alcohols via Addition Reactions

Overview
The acid-catalyzed addition of water to the double bond of alkenes is a large-scale industrial method used to synthesize low-molecular-weight alcohols. An acidic atmosphere is required to allow the hydrogen in the water molecule to act as an electrophile and attack the double bond in an alkene. The addition of a proton to the double bond creates a carbocation intermediate. The proton preferentially bonds to the less substituted end of the double bond to create a more stable carbocation...
Aldehydes and Ketones with Alcohols: Hemiacetal Formation01:19

Aldehydes and Ketones with Alcohols: Hemiacetal Formation

Similar to water, alcohols can add to the carbonyl carbon of the aldehydes and ketones. The addition of one molecule of alcohol to the carbonyl compound forms the hemiacetal or half acetal. As depicted below, in a hemiacetal, the carbon is directly linked to an OH and OR group.
Oxidation of Alcohols02:37

Oxidation of Alcohols

In this lesson, the oxidation of alcohols is discussed in depth. The various reagents used for oxidation of primary and secondary alcohols are detailed, and their mechanism of action is provided.
The process of oxidation in a chemical reaction is observed in any of the three forms:
Conversion of Alcohols to Alkyl Halides02:48

Conversion of Alcohols to Alkyl Halides

This lesson delves into the conversion of alcohols to corresponding alkyl halides and the mechanism of action for different reagents. Typically, the hydroxyl group is first protonated to convert it to a stable leaving group. Consequently, based on the starting alcohol, the mechanism undergoes either of the nucleophilic substitution routes, SN1 or SN2. Tertiary alkyl halides are made using the two-step SN1 mechanism that occurs via a carbocation intermediate, which is stabilized by...
Regioselectivity and Stereochemistry of Acid-Catalyzed Hydration02:34

Regioselectivity and Stereochemistry of Acid-Catalyzed Hydration

The rate of acid-catalyzed hydration of alkenes depends on the alkene's structure, as the presence of alkyl substituents at the double bond can significantly influence the rate.

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A Toolkit to Enable Hydrocarbon Conversion in Aqueous Environments
20:28

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Published on: October 2, 2012

Conformational changes and catalysis by alcohol dehydrogenase.

Bryce V Plapp1

  • 1Department of Biochemistry, The University of Iowa, Iowa City, IA 52242-1109, USA. bv-plapp@uiowa.edu

Archives of Biochemistry and Biophysics
|July 9, 2009
PubMed
Summary

Horse liver alcohol dehydrogenase undergoes a significant conformational change when binding coenzymes like NAD(+) or NADH. This dynamic shift optimizes the active site for efficient catalysis, highlighting protein dynamics in enzyme function.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzyme Kinetics

Background:

  • Horse liver alcohol dehydrogenase (ADH) is a key enzyme in alcohol metabolism.
  • Enzyme catalysis is often regulated by conformational changes.
  • Understanding these dynamics is crucial for enzyme mechanism elucidation.

Purpose of the Study:

  • To investigate the global conformational changes in horse liver ADH upon coenzyme binding.
  • To elucidate the role of these conformational changes in catalytic efficiency.
  • To explore the kinetic and mechanistic details of coenzyme binding and substrate interaction.

Main Methods:

  • X-ray crystallography was used to determine enzyme structures.
  • Kinetic analyses were performed to study reaction rates.
  • Site-directed mutagenesis and chemical modifications were employed to probe specific residues.

Main Results:

  • Coenzyme binding (NAD(+) or NADH) induces a global conformational change involving domain rotation and active site closure.
  • This conformational change is essential for catalytic efficiency and is influenced by coenzyme saturation.
  • The binding of NAD(+) is rate-limited by a unimolecular isomerization step involving zinc-hydroxide deprotonation, facilitated by His-51.
  • Substrate binding involves displacement of the zinc-bound hydroxide, potentially via a double displacement mechanism.
  • Hydride transfer may occur via quantum mechanical tunneling, influenced by protein dynamics.

Conclusions:

  • Protein dynamics, specifically global conformational changes, are critical for alcohol dehydrogenase catalysis.
  • The enzyme's active site undergoes significant structural rearrangements to optimize substrate binding and facilitate hydride transfer.
  • These findings provide insights into the intricate mechanisms of enzyme-substrate interactions and catalytic turnover.