The active site structure of E. coli HPII catalase : Evidence favoring coordination of a tyrosinate proximal ligand to the chlorin iron

E. coli produces 2 catalases known as HPI and HPII. While the heme prosthetic group of the HPII catalase has been established to be a dihydroporphyrin or chlorin, the identity of the proximal ligand to the iron has not been addressed. The magnetic circular dichroism (MCD) spectrum of native ferric H...

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Bibliographic Details
Published in:	FEBS letters Vol. 295; no. 1; pp. 123 - 126
Main Authors:	Dawson, John H., Bracete, Alma M., Huff, Ann M., Kadkhodayan, Saloumeh, Zeitler, Caroline M., Sono, Masanori, Chang, Chi K., Loewen, Peter C.
Format:	Journal Article
Language:	English
Published:	Amsterdam Elsevier B.V 16-12-1991 Elsevier
Subjects:	Active site structure determination Analytical, structural and metabolic biochemistry Binding Sites Biological and medical sciences Catalase Catalase - chemistry Catalase - metabolism Circular Dichroism Dihydroporphyrin Electron Spin Resonance Spectroscopy Enzymes and enzyme inhibitors EPR spectroscopy Escherichia coli - enzymology Fundamental and applied biological sciences. Psychology Isoenzymes - chemistry Isoenzymes - metabolism Magnetic circular dichroism spectroscopy Oxidoreductases Porphyrins Protein Conformation Tyrosinate proximal ligand Tyrosine Tyrosinate proximal ligand Active site structure determination Catalase Magnetic circular dichroism spectroscopy EPR HRP Dihydroporphyrin MeC OEC EPR spectroscopy MCD Enzyme Isozyme Escherichia coli Active site EPR spectrometry Bacteria Magnetic circular dichroism Enterobacteriaceae Structural analysis
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