Electron spin echo envelope modulation spectroscopic study of iron-nitrogen interactions in myoglobin hydroxide and Fe(III) tetraphenylporphyrin models.
The electron-nuclear coupling in low-spin iron complexes including myoglobin hydroxide (MbOH) and two related model compounds, Fe(III) tetraphenylporphyrin(pyridine)(OR-) (R = H or CH3) and Fe(III) tetraphenylporphyrin(butylamine)(OR-) was investigated using electron spin echo envelope modulation (ESEEM) spectroscopy. The assignment of frequency components in ESEEM spectra was accomplished through the use of nitrogen isotopic substitution wherever necessary. For example, the proximal imidazole coupling in MbOH was investigated without interference from the contributions of porphyrin 14N nuclei after substitution of the heme in native Mb with 15N-labeled heme. Computer simulation of spectra using angle selected techniques enabled the assignment of parameters describing the hyperfine and quadrupole interactions for axially bound nitrogen of imidazole in MbOH, of axial pyridine and butylamine in the models, and for the porphyrin nitrogens of the heme in native MbOH. The isotropic component of axial nitrogen hyperfine interactions exhibits a trend from 5 to 4 MHz, with imidazole (MbOH) greater than pyridine greater than amine. The nuclear quadrupole interaction coupling constant e2Qq was near 2 MHz for all nitrogens in these complexes. The Qzz axis of the nuclear quadrupole interaction tensor for the proximal imidazole nitrogen in MbOH was found to be aligned near gz (gmax) in MbOH, suggesting that gz is near the heme normal. A crystal field analysis, that allows a calculation of rhombic and axial splittings for the d orbitals of the t2g set in a low-spin heme complex, based on the g tensor assignment gz greater than gy greater than gx, yielded results that are consistent with the poor pi-acceptor properties expected for the closed shell oxygen atom of the hydroxide ligand in MbOH. A discussion is presented of the unusual results reported in a linear electric field effect in EPR (LEFE) study of MbOH published previously [Mims, W. B., & Peisach, J. (1976) J. Chem. Phys. 64, 1074-1091].
Magliozzo
R S
RS
Department of Molecular Pharmacology, Albert Einstein College of Medicine, Yeshiva University, Bronx, New York 10461.
Peisach
J
J
D000818:Animals; D002082:Butylamines / Q000737:chemistry; D003198:Computer Simulation; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D005290:Ferric Compounds / Q000737:chemistry* / Q000378:metabolism; D006736:Horses; D008024:Ligands; D008665:Metalloporphyrins / Q000737:chemistry*; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry* / Q000378:metabolism; D009584:Nitrogen / Q000737:chemistry* / Q000378:metabolism; D011725:Pyridines / Q000737:chemistry
D002082:Butylamines; D005290:Ferric Compounds; D008024:Ligands; D008665:Metalloporphyrins; D009211:Myoglobin; D011725:Pyridines; C032547:iron tetraphenylporphyrin; D009584:Nitrogen; C023666:pyridine