Title
Marked difference in the electronic structure of cyanide-ligated ferric protoglobins and myoglobin due to heme ruffling Marked difference in the electronic structure of cyanide-ligated ferric protoglobins and myoglobin due to heme ruffling
Author
Faculty/Department
Faculty of Sciences. Physics
Faculty of Pharmaceutical, Biomedical and Veterinary Sciences . Biomedical Sciences
Publication type
article
Publication
Easton, Pa ,
Subject
Chemistry
Source (journal)
Inorganic chemistry / American Chemical Society. - Easton, Pa
Volume/pages
51(2012) :16 , p. 8834-8841
ISSN
0020-1669
ISI
000307606200029
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Affiliation
University of Antwerp
Abstract
Electron paramagnetic resonance experiments reveal a significant difference between the principal g values (and hence, ligand-field parameters) of the ferric cyanide-ligated form of different variants of the protoglobin of Methanosarcina acetivorans (MaPgb) and of horse heart myoglobin (hhMb). The largest principal g value of the ferric cyanide-ligated MaPgb variants is found to be significantly lower than for any of the other globins reported so far. This is at least partially caused by the strong heme distortions as proven by the determination of the hyperfine interaction of the heme nitrogens and mesoprotons. Furthermore, the experiments confirm recent theoretical predictions [Forti, F.; Boechi, L., Bikiel, D., Marti, M.A.; Nardini, M.; Bolognesi, M.; Viappiani, C.; Estrin, D.; Luque, F. J. J. Phys. Chem. B 2011, 115, 13771-13780] that Phe(G8)145 plays a crucial role in the ligand modulation in MaPgb. Finally, the influence of the N-terminal 20 amino-acid chain on the heme pocket in these protoglobins is also proven.
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