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Preparation and Cryo-FIB micromachining of Saccharomyces cerevisiae for Cryo-Electron Tomography
Published on: November 20, 2021
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Metal binding to Saccharomyces cerevisiae ferrochelatase
Tobias Karlberg1, David Lecerof, Monika Gora
1Department of Molecular Biophysics, Centre for Chemistry and Chemical Engineering, Lund University, Sweden.
Biochemistry
|November 13, 2002
Summary
Ferrochelatase enzyme structures reveal asymmetric metal binding sites. H235 is the primary iron binding residue, with a secondary regulatory site identified.
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- Ferrochelatase is the final enzyme in heme biosynthesis, catalyzing iron insertion into protoporphyrin IX.
- Understanding ferrochelatase structure is crucial for elucidating heme pathway regulation.
Purpose of the Study:
- To determine the crystal structures of Saccharomyces cerevisiae ferrochelatase.
- To characterize metal binding sites and inhibitor interactions.
Main Methods:
- X-ray crystallography was used to obtain structures of free ferrochelatase and its complexes with Co(II), Cd(II), and Hg(I).
- Analysis of protein-metal interactions and identification of key amino acid residues involved in catalysis and regulation.
Main Results:
- Ferrochelatase exists as a homodimer with asymmetric monomeric units.
- A primary metal binding site involving H235, E314, and S275 was identified, with H235 as the principal metal-coordinating residue.
- A secondary, surface-exposed metal binding site involving E97, H317, and E326 was discovered, potentially involved in regulation.
Conclusions:
- The asymmetric structure influences metal binding and substrate processing.
- H235 is critical for catalytic iron insertion.
- The secondary binding site may play a role in enzyme regulation, analogous to magnesium binding in other ferrochelatases.
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