Literature summary for 4.98.1.1 extracted from

Bencze, K.Z.; Yoon, T.; Millan-Pacheco, C.; Bradley, P.B.; Pastor, N.; Cowan, J.A.; Stemmler, T.L.
Human frataxin: Iron and ferrochelatase binding surface (2007), Chem. Commun. (Camb. ), 18, 1798-1800.

No PubMed abstract available

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Co2+	-	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	frataxin binds at nanomolar affinity to the ferrochelatase and the iron-sulfur cluster assembly apparatus, monomeric frataxin interacts with the ferrochelatase dimer predominantly utilizing frataxins helical surface, including iron binding residues in the helix-1/strand-1 conserved acidic residue patch of the protein	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
dimer	-	Homo sapiens

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Release 2023.1 (January 2023)