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Oxidation of Alkenes: Syn Dihydroxylation with Osmium Tetraoxide

Oxidation of Alkenes: Syn Dihydroxylation with Osmium Tetraoxide

Alkenes are converted to 1,2-diols or glycols through a process called dihydroxylation. It involves the addition of two hydroxyl groups across the double bond with two different stereochemical approaches, namely anti and syn. Dihydroxylation using osmium tetroxide progresses with syn stereochemistry.

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Diols are compounds with two hydroxyl groups. In addition to syn dihydroxylation, diols can also be synthesized through the process of anti dihydroxylation. The process involves treating an alkene with a peroxycarboxylic acid to form an epoxide. Epoxides are highly strained three-membered rings with oxygen and two carbons occupying the corners of an equilateral triangle. This step is followed by ring-opening of the epoxide in the presence of an aqueous acid to give a trans diol.

Oxidations of Aldehydes and Ketones to Carboxylic Acids

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Oxidation of aldehydes and ketones results in the formation of carboxylic acids. Aldehydes, bearing hydrogen next to the carbonyl group, are easily oxidized compared to ketones. This is because an aldehydic proton can easily be abstracted during oxidation.
Aldehydes readily undergo oxidation in strong oxidizing agents such as potassium permanganate and chromic acid. The oxidation can also be carried out using mild oxidizing agents such as silver oxide. In fact, aldehydes can be easily oxidized...

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Introduction
One of the convenient methods for the preparation of aldehydes and ketones is via hydration of alkynes. Hydroboration-oxidation of alkynes is an indirect hydration reaction in which an alkyne is treated with borane followed by oxidation with alkaline peroxide to form an enol that rapidly converts into an aldehyde or a ketone. Terminal alkynes form aldehydes, whereas internal alkynes give ketones as the final product.

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Related Experiment Video

Updated: Jun 26, 2026

A Direct, Regioselective and Atom-Economical Synthesis of 3-Aroyl-N-hydroxy-5-nitroindoles by Cycloaddition of 4-Nitronitrosobenzene with Alkynones

A Direct, Regioselective and Atom-Economical Synthesis of 3-Aroyl-N-hydroxy-5-nitroindoles by Cycloaddition of 4-Nitronitrosobenzene with Alkynones

Published on: January 21, 2020

A comparative study of hydroxyindole oxidases.

H Blaschko, W G Levine

British Journal of Pharmacology and Chemotherapy

|December 25, 2008

Summary

This study compares Mytilus edulis gill plate oxidase and mammalian caeruloplasmin, finding both oxidize hydroxyindoles. Caeruloplasmin shows more restricted substrate specificity than the Mytilus enzyme.

Area of Science:

Biochemistry
Enzymology
Comparative Biology

Background:

Oxidation of 5-hydroxytryptamine (5-HT) and related compounds is catalyzed by various oxidases.
Caeruloplasmin, a copper-containing oxidase in mammalian plasma, and an oxidase from Mytilus edulis gill plates are key enzymes in this process.
Understanding the substrate specificity of these enzymes is crucial for elucidating their biological roles.

Purpose of the Study:

To comparatively analyze the oxidation of 5-hydroxytryptamine and related indole derivatives by Mytilus edulis gill plate oxidase and mammalian caeruloplasmin.
To determine the substrate specificity of both enzymes and identify similarities and differences in their catalytic activities.
To investigate the nature of the Mytilus edulis gill plate oxidase.

Main Methods:

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Comparative enzymatic assays using 5-hydroxytryptamine and a range of substituted indole derivatives as substrates.
Characterization of oxidation products, including colorimetric analysis (blue and brown pigments).
Testing the effects of specific inhibitors (e.g., copper enzyme inhibitors, edetate, carbon monoxide) on enzyme activity.

Main Results:

Both Mytilus edulis oxidase and caeruloplasmin oxidized indole derivatives with hydroxyl groups at the 4-, 5-, 6-, or 7- positions.
Psilocine (4-hydroxyindole derivative) was rapidly oxidized by both enzymes, yielding a blue color, while bufotenine (5-hydroxyindole derivative) produced brown pigments.
The Mytilus enzyme exhibited broader substrate specificity, oxidizing hydroxytryptophan and 5-hydroxyindole derivatives, which were not substrates for caeruloplasmin.

Conclusions:

The Mytilus edulis gill plate oxidase and mammalian caeruloplasmin catalyze similar oxidation reactions, acting as 'hydroxyindole oxidases'.
Caeruloplasmin demonstrates a more restricted substrate specificity compared to the Mytilus enzyme.
The Mytilus enzyme's activity is inhibited by copper enzyme inhibitors but not by edetate or carbon monoxide, suggesting a copper-dependent mechanism distinct from amine oxidase activity.