The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis

Autor:	C K, Wu, H A, Dailey, J P, Rose, A, Burden, V M, Sellers, B C, Wang
Rok vydání:	2001
Předmět:	Iron-Sulfur Proteins Models Molecular Binding Sites Detergents Molecular Sequence Data Heme Crystallography X-Ray Catalysis Protein Structure Secondary Metals Mutation Humans Amino Acid Sequence Dimerization Sequence Alignment Ferrochelatase
Zdroj:	Nature structural biology. 8(2)
ISSN:	1072-8368
Popis:	Human ferrochelatase (E.C. 4.99.1.1) is a homodimeric (86 kDa) mitochondrial membrane-associated enzyme that catalyzes the insertion of ferrous iron into protoporphyrin to form heme. We have determined the 2.0 A structure from the single wavelength iron anomalous scattering signal. The enzyme contains two NO-sensitive and uniquely coordinated [2Fe-2S] clusters. Its membrane association is mediated in part by a 12-residue hydrophobic lip that also forms the entrance to the active site pocket. The positioning of highly conserved residues in the active site in conjunction with previous biochemical studies support a catalytic model that may have significance in explaining the enzymatic defects that lead to the human inherited disease erythropoietic protoporphyria.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::7097c4a0917db500ac11f18a26fdddfc https://pubmed.ncbi.nlm.nih.gov/11175906 Zobrazit plný text záznamu Full text from SpringerLink