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Updated: Aug 18, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
Published on: July 9, 2015
Heme methyl 1H chemical shifts as structural parameters in some low-spin ferriheme proteins
I Bertini1, C Luchinat, G Parigi
1Center for Magnetic Resonance, Department of Chemistry, University of Florence, Italy. bertini@cerm.unifi.it
Abstract:
The different paramagnetic shifts of the four methyl groups in ferriheme proteins have been described as being due to the effect of the axial ligand nodal plane orientation. An equation, heuristically found and theoretically explained, describing the relation between contact and pseudocontact shifts and the position of the axial ligand(s) has been derived for bis-histidine ferriheme proteins and for cyanide-histidine ferriheme proteins. The values of the heuristic parameters contained in the equations were found by fitting the shifts of bovine cytochrome b5 and several bis-histidine cytochromes c3 and histidine-cyanide systems. The agreement between the observed and the calculated shifts was found to be good. Therefore, by taking advantage of this study, information on the position of the axial ligands, that can be used as a constraint for structure determination, can be obtained from the shifts of the methyl protons.
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