NDLI: Resonance Raman investigation of dioxygen bonding in oxycobaltmyoglobin and oxycobalthemoglobin: structural implication of splittings of the bound O--O stretching vibration.

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Resonance Raman investigation of dioxygen bonding in oxycobaltmyoglobin and oxycobalthemoglobin: structural implication of splittings of the bound O--O stretching vibration.

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Resonance Raman investigation of dioxygen bonding in oxycobaltmyoglobin and oxycobalthemoglobin: structural implication of splittings of the bound O--O stretching vibration.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Tsubaki, M. Yu, N. T.
Abstract	Splittings related to the stretching vibration of bound dioxygen in hemoproteins have been detected by resonance Raman spectroscopy. With excitation at 406.7 nm we observe three isotope-sensitive lines in oxycobaltmyoglobin (oxyCoMb) [or in oxycobalthemoglobin A (oxyCoHbA)] at 1103 (1107), 1137 (1137), and 1153 (1152) cm-1, of which the most intense one appears at 1137 cm-1. The first two frequencies arise from resonance interaction between a v(O--O) mode at approximately 1122 cm-1 and an accidentally degenerate porphyrin ring mode at 1123 (1121) cm-1, whereas the third one represents an 'unperturbed' v(O--O) vibration from a different species. These two v(O--O) modes at approximately 1122 and approximately 1153 cm-1 shift to approximately 1066 and approximately 1096 cm-1, respectively, upon 16O2 leads to 18O2 substitution. The same resonance interaction may also occur in oxyFeMb (probably also in oxyFeHb(a), because it exhibits an intensity increase at 1125 cm-1 upon 16O2 leads to 18O2 substitution, although the v(O--O) vibrations have not been observed directly. Concomitant enhancement is observed in the v(Co--O) vibration at 539 (537( cm-1, which is considerably lower than the v(Fe--O) frequency at approximately 570 cm-1 in oxyFeMb and oxyFeHbA. The Co--O bond is longer and weaker than the Fe--O bond. Enhancement of both v(O--O) and v(Co--O) indicates the existence of a charge-transfer transition underlying the Soret band, which may be assigned as pi(pi gO2/xz) leads to sigma(dz2Co/pi g). The presence of two v(O--O) vibrations (at approximately 1122 and approximately 1152 cm-1) but only one v(Co--O) mode at approximately 538 cm-1) means that the two species in oxyCoMB or oxyCoHbA have the same Co--O bond lengths but different O--O bond lengths. The bound dioxygen in a bent end-on configuration may have two allowed orientations, which differ in the extent of sp2(N epsilon) leads to pi*(O2) donation from distal histidine.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	6
Volume Number	78
Language	English
Publisher	National Academy of Sciences
Publisher Date	1981-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cobalt Myoglobin Oxygen Oxyhemoglobins Animals Chemical Phenomena Chemistry, Physical Macromolecular Substances Motion Spectrum Analysis, Raman Whales Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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