Lipoxygenases: structural principles and spectroscopy

Gaffney, B.J. (1996) Lipoxygenases: structural principles and spectroscopy. Annual Review of Biophysics and Biomolecular Structure, 25. pp. 431-459.

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Abstract

poxygenases catalyze the formation of fatty acid hydroperoxides, products used in further biochemical reactions leading to normal and pathological cell functions. X-ray structure analysis and spectroscopy have been applied to elucidate the mechanism of lipoxygenases. Two X-ray structures of soybean lipoxygenase-1 reveal the side chains of three histidines and the COO- of the carboxy terminus as ligands to the catalytically important iron atom. The enzyme contains a novel three-turn pi-helix near the iron center. Spectroscopic studies, including electron magnetic resonance, X-ray absorption spectroscopy, infrared circular dichroism, and magnetic circular dichroism, have been applied to compare lipoxygenases from varied sources and with different substrate positional specificity.

Item Type: Article
Author Affiliation: John hopkins Universit, Baltimore, Maryland
Subjects: Plant Physiology and Biochemistry > Plant Physiology
Plant Physiology and Biochemistry > Biochemistry
Divisions: Millet
Depositing User: Library ICRISAT-InfoSAT
Date Deposited: 12 Apr 2012 04:50
Last Modified: 12 Apr 2012 04:51
URI: http://eprints.icrisat.ac.in/id/eprint/4648

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