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Infrared spectroscopic evidence of hydrogen bonding between carbon monoxide and protein in carbonylhorseradish peroxidase C
Author(s) -
Smith Michael L.,
Ohlsson Per-Ingvar,
Paul Karl Gustav
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80840-0
Subject(s) - carbon monoxide , chemistry , infrared , hydrogen bond , peroxidase , hydrogen , infrared spectroscopy , oxygen , crystallography , ligand (biochemistry) , photochemistry , molecule , enzyme , catalysis , biochemistry , organic chemistry , receptor , physics , optics
Carbonylhorseradish peroxidase isoenzyme C 2 (EC 1.11.1.7) exhibits two bands in the infrared spectrum attributable to the ligand CO at 1933.5 and 1905 cm −1 . Replacement of H 2 O by D 2 O results in shifts to both bands to new positions at 1932.5 and 1902.5 cm −1 . The results indicate strong hydrogen bonding to the terminal oxygen of CO, of strength comparable to that recently observed for oxyhemoglobin and oxymyoglobin.