The reactivity of cytochrome c with soft ligands

The spectral changes caused by binding soft ligands to the cytochrome c iron and their correlation to ligand affinities support the hypothesis that the iron—methionine sulfur bond of this heme protein is enhanced by delocalization of the metal l 2, electrons into the empty 3d orbitals of the ligand...

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Veröffentlicht in:	FEBS letters 1991-03, Vol.280 (2), p.199-201
Hauptverfasser:	Schejter, Abel, Plotkin, Batya, Vig, Ida
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Animals Binding Sites Biological and medical sciences Cytochrome c Cytochrome c Group - chemistry Fundamental and applied biological sciences. Psychology Hemoproteins Horses Iron-Sulfur Proteins - chemistry Iron—sulfur bond Ligands Metalloproteins Myocardium - enzymology Proteins Soft ligands Spectrophotometry
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Beschreibung
Zusammenfassung:	The spectral changes caused by binding soft ligands to the cytochrome c iron and their correlation to ligand affinities support the hypothesis that the iron—methionine sulfur bond of this heme protein is enhanced by delocalization of the metal l 2, electrons into the empty 3d orbitals of the ligand atom. These findings also explain the unique spectrum of cytochrome c in the far red.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(91)80292-B