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Saccharomyces cerevisiae ferrochelatase forms a homodimer.

Archives of biochemistry and biophysics - 15 Feb 2002

Grzybowska Ewa, Góra Monika, Plochocka Danuta, Rytka Joanna

Abstract excerpt

Ferrochelatase, the last enzyme of the heme biosynthetic pathway, has for years been considered to be active as a monomer. The crystal structure of Bacillus subtilis ferrochelatase confirmed its monomeric structure. However, animal ferrochelatase was found to form a functional dimer. Data presented here indicate that ferrochelatase from the yeast Saccharomyces cerevisiae is also dimeric. Following two-hybrid...

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PMID: 11831847
DOI: 10.1006/abbi.2001.2730

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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