Site-Directed Mutagenesis and Spectroscopic Characterization of Human Ferrochelatase: Identification of Residues Coordinating the [2Fe-2S] Cluster

The five cysteines closest to the carboxyl terminus of human ferrochelatase have been individually mutated to serine, histidine, or aspartate residues in an attempt to identify the protein ligands to the [2Fe-2S] cluster. Mutations of cysteines at positions 403, 406, and 411 (C403D, C403H, C406D, C4...

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Veröffentlicht in:	Biochemistry (Easton) 1996-12, Vol.35 (50), p.16222-16229
Hauptverfasser:	Crouse, Brian R, Sellers, Vera M, Finnegan, Michael G, Dailey, Harry A, Johnson, Michael K
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Cattle Cloning, Molecular Cysteine Dithionite Electron Spin Resonance Spectroscopy Escherichia coli Ferrochelatase - biosynthesis Ferrochelatase - chemistry Ferrochelatase - isolation & purification Humans Iron-Sulfur Proteins - biosynthesis Iron-Sulfur Proteins - chemistry Iron-Sulfur Proteins - isolation & purification Mice Molecular Sequence Data Mutagenesis, Site-Directed Oxidation-Reduction Protein Conformation Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Sequence Homology, Amino Acid Spectrum Analysis, Raman
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