Abstract:
:We have obtained the 470 MHz 19F NMR spectra of wild type [4-F]Trp-labeled myoglobins (MbCO, MbO2, deoxyMb, metMb, and MbCN) and hemoglobins (HbCO, HbO2, and deoxyHb), as well as those of several mutants (W7F Mb, betaW15F Hb, betaW37S Hb, and betaY130F Hb, all as the carbonmonoxy adducts), prepared via site-directed mutagenesis. The maximum observed chemical shift range induced by folding is 6.4 ppm. Using a multipole shielding polarizability-local reaction field approach, we have computed the electrostatic field contributions to the fluorine shielding. For residues which do not have F atoms in contact with neighboring groups, we find an approximately 1 ppm mean square deviation in shift from experiment, with the R2-like structure of HbCOA being in very close accord with experiment.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Pearson JG,Montez B,Le H,Oldfield E,Chien EY,Sligar SGdoi
10.1021/bi961664hsubject
Has Abstractpub_date
1997-03-25 00:00:00pages
3590-9issue
12eissn
0006-2960issn
1520-4995pii
bi961664hjournal_volume
36pub_type
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