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Related Experiment Video

Updated: Jun 21, 2025

A Rapid and Specific Microplate Assay for the Determination of Intra- and Extracellular Ascorbate in Cultured Cells

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Published on: April 11, 2014

Direct Spectroscopic Ferrochelatase Assay.

Harry A Dailey^1,2, Amy E Medlock^3,4

¹Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, USA.

Methods in Molecular Biology (Clifton, N.J.)

|July 15, 2024

Summary

We developed a fast, direct spectroscopic assay to measure ferrochelatase activity. This new method quantifies the enzyme

Keywords:

Chelation Ferrochelatase Heme biosynthesis Iron Porphyrin

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Area of Science:

Biochemistry
Enzymology

Background:

Ferrochelatases (EC 4.99.1.1) are crucial enzymes.
They catalyze the final step in heme biosynthesis.
Measuring ferrochelatase activity is important for understanding heme metabolism and related disorders.

Purpose of the Study:

To develop a novel, rapid, real-time assay for ferrochelatase activity.
To provide a direct spectroscopic method for measuring both protoporphyrin and coproporphyrin ferrochelatases.

Main Methods:

Development of a direct spectroscopic assay.
Utilizing real-time measurement of enzyme activity.
Testing the assay with both protoporphyrin IX and coproporphyrin III substrates.

Main Results:

A rapid, real-time, direct spectroscopic assay for ferrochelatase was established.
The assay successfully measured ferrochelatase activity using both protoporphyrin and coproporphyrin substrates.
This method offers a significant improvement over existing assays.

Conclusions:

The described assay provides a robust and efficient tool for studying ferrochelatase.
This new method facilitates research into heme biosynthesis and associated diseases.