Multinuclear (13C, 17O, 57Fe) NMR studies of carbonmonoxy heme proteins and synthetic model compounds

Charalampos G. Kalodimos, Ioannis P. Gerothanassis, Roberta Pierattelli, Anastasios Troganis

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8 Scopus citations

Abstract

13C, 17O and 57Fe NMR spectra of several carbonmonoxy hemoprotein models with varying polar and steric effects of the distal organic superstructure, constraints of the proximal side, and porphyrin ruffling are reported. Both heme models and heme proteins obey a similar excellent linear δ(13C) versus ν(C-O) relationship which is primarily due to modulation of π-back-bonding from the Fe d(π) to CO π* orbital by the distal pocket polar interactions. The lack of correlation between δ(13C) and δ(17O) suggests that the two probes do not reflect a similar type of electronic and structural perturbation. δ(17O) is not primarily influenced by the local distal field interactions and does not correlate with any single structural property of the Fe-C-O unit; however, atropisomerism and deformation of the porphyrin geometry appear to play a significant role. 57Fe shieldings vary by nearly 900 ppm among various hemes and an excellent correlation was found between δ(57Fe) and the absolute crystallographic average displacement of the meso carbon atoms, |C(m)|, relative to the porphyrin core mean plane. The excellent correlation between iron-57 shieldings and the average shieldings of the meso carbons of the porphyrin skeleton of TPP derivatives suggests that the two probes reflect a similar type of electronic and structural perturbation which is primarily porphyrin ruffling. (C) 2000 Elsevier Science Inc.

Original languageEnglish (US)
Pages (from-to)371-380
Number of pages10
JournalJournal of Inorganic Biochemistry
Volume79
Issue number1-4
DOIs
StatePublished - Apr 30 2000

Bibliographical note

Funding Information:
This research was supported by the Greek General Secretariat of Research and Technology, a Greek–Italian collaborative Research Grant (1999-2001), EMBO (Short Term Fellowship to C.G.K.), FEBS (Short Term Fellowship to C.G.K.), and the Greek Scholarship Foundation (Ph.D. research Fellowship to C.G.K.). We wish to thank the EU-Large Scale PARABIO Facility at the University of Florence for the use of the Bruker AVANCE-600 instrument and the ULIRS facility located at QMC, University of London, for the use of the Bruker AMX-600 instrument.

Keywords

  • Hemoproteins
  • Multinuclear magnetic resonance spectroscopy
  • Synthetic model compounds

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