The H93G myoglobin cavity mutant as a versatile scaffold for modeling heme iron coordination structures in protein active sites and their characterization with magnetic circular dichroism spectroscopy

• Published in: Coordination chemistry reviews Vol. 255; no. 7; pp. 700 - 716
• Main Authors: Du, Jing, Sono, Masanori, Dawson, John H.
• Format: Journal Article
• Language: English
• Published: Switzerland Elsevier B.V 01.04.2011
• Subjects: Cavity mutant; H93G Mb; Heme protein active site models; MCD spectroscopy; H93G; Im; Cavity mutant; P420; K d; C420; Heme protein active site models; ccNiR; Shp; MCD spectroscopy; Cyt P450; BME; WT; CPSH; CooA; CD; THT; 4Me-Im; H93G Mb; Py; CAM; MCD; MPs; CCP; UV–Vis; Mb; CHA

Preparation of heme model complexes is a challenging subject of long-standing interest for inorganic chemists. His93Gly sperm whale myoglobin (H93G Mb) has the proximal His replaced with the much smaller non-coordinating Gly. This leaves a cavity on the proximal side of the heme into which a wide va...