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Titolo:
NMR, IR, Mossbauer and quantum chemical investigations of metalloporphyrins and metalloproteins
Autore:
Sanders, LK; Arnold, WD; Oldfield, E;
Indirizzi:
Univ Illinois, Dept Chem, Urbana, IL 61801 USA Univ Illinois Urbana IL USA 61801 linois, Dept Chem, Urbana, IL 61801 USA
Titolo Testata:
JOURNAL OF PORPHYRINS AND PHTHALOCYANINES
fascicolo: 3, volume: 5, anno: 2001,
pagine: 323 - 333
SICI:
1088-4246(200103)5:3<323:NIMAQC>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; DENSITY-FUNCTIONAL THEORY; SOLID-STATE NMR; FE-C-O; POCKET DOCKING SITE; CARBON-MONOXIDE; HEME-PROTEINS; QUADRUPOLE SPLITTINGS; SHIELDING TENSORS; ANALOG METALLOPORPHYRINS;
Keywords:
hemoglobin; myoglobin; NMR; IR; Mossbauer; X-ray; density functional theory (DFT); metalloporphyrins; metalloproteins;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
101
Recensione:
Indirizzi per estratti:
Indirizzo: Oldfield, E Univ Illinois, Dept Chem, 600 S Mathews Ave, Urbana, IL 61801 USA Univ Illinois 600 S Mathews Ave Urbana IL USA 61801 61801 USA
Citazione:
L.K. Sanders et al., "NMR, IR, Mossbauer and quantum chemical investigations of metalloporphyrins and metalloproteins", J PORPHYR P, 5(3), 2001, pp. 323-333

Abstract

We review contributions made towards the elucidation of CO and O-2 bindinggeometries in respiratory proteins. Nuclear magnetic resonance, infrared spectroscopy, Mossbauer spectroscopy, X-ray crystallography and quantum chemistry have all been used to investigate the Fe-ligand interactions. Early experimental results showed linear correlations between O-17 chemical shiftsand the infrared stretching frequency (VCO) Of the CO ligand in carbonmonoxyheme proteins and between the O-17 chemical shift and the (CO)-C-13 shift. These correlations led to early theoretical investigations of the vibrational frequency of carbon monoxide and of the C-13 and O-17 NMR chemical shifts in the presence of uniform and non-uniform electric fields. Early success in modeling these spectroscopic observables then led to the use of computational methods, in conjunction with experiment, to evaluate ligand-binding geometries in heme proteins. Density functional theory results are described which predict Fe-57 chemical shifts and Mossbauer electric field gradient tensors,O-17 NMR isotropic chemical shifts, chemical shift tensors and nuclear quadrupole coupling constants (e(2)qQ/h) as well as C-13 isotropic chemical shifts and chemical shift tensors in organometallic clusters, heme model metalloporphyrins and in metalloproteins. A principal result is that CO in most heme proteins has an essentially linear and untilted geometry (tau = 4 degrees, beta = 7 degrees) which is in extremely good agreement witha recently published X-ray synchrotron structure. CO/O-2 discrimination isthus attributable to polar interactions with the distal histidine residue,rather than major Fe-C-O geometric distortions. Copyright (C) 2001 John Wiley & Sons, Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 12:25:14