Identification of heme macrocycle type by near-infrared magnetic circular dichroism spectroscopy at cryogenic temperatures.
The electron paramagnetic resonance (EPR) and near-infrared magnetic circular dichroism (MCD) spectra of the azide and cyanide adducts of nitrimyoglobin and hydroperoxidase II from Escherichia coli have been measured at cryogenic temperatures. For the first time, ligand-to-metal charge-transfer transitions in the near-infrared have been observed for an Fe(III)-chlorine system. It is shown that near-ultraviolet-to-visible region electronic spectra of 'green' hemes such as these are an unreliable indicator of macrocycle type. However, the combined application of EPR and near-infrared MCD spectroscopies clearly distinguishes between the porphyrin-containing nitrimyoglobin and the chlorine-containing hydroperoxidase II.
Peng
Q
Q
Department of Chemistry, University of Alabama, Tuscaloosa 35487-0336.
Timkovich
R
R
Loewen
P C
PC
Peterson
J
J
D002942:Circular Dichroism; D003080:Cold Temperature; D004578:Electron Spin Resonance Spectroscopy; D006418:Heme / Q000737:chemistry / Q000145:classification*; D009211:Myoglobin / Q000737:chemistry*; D009195:Peroxidase / Q000737:chemistry*; D011166:Porphyrins / Q000737:chemistry
D009211:Myoglobin; D011166:Porphyrins; C006969:chlorin; D006418:Heme; D009195:Peroxidase