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Low frequency resonance Raman spectra of isolated α and β subunits of hemoglobin and their deuterated analogues
Author(s) -
Podstawka Edyta,
Mak Piotr J.,
Kincaid James R.,
Proniewicz Leonard M.
Publication year - 2006
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20573
Subject(s) - chemistry , deuterium , raman spectroscopy , stereochemistry , heme , hemeprotein , computational chemistry , crystallography , organic chemistry , atomic physics , physics , optics , enzyme
Abstract In an attempt to gain further insight into the nature of the low frequency vibrational modes of hemoglobin and its isolated subunits, a comprehensive study of several different isotopically labeled analogues has been undertaken and is reported herein. Specifically, the resonance Raman spectra, between 200 and 500 cm −1 , are reported for the deoxy and ligated (CO and O 2 ) forms of the isolated α and β subunits containing the natural abundance or various deuterated analogues of protoheme. The deuterated protoheme analogues studied include the 1,3,5,8‐C 2 H 3 ‐protoheme ( d 12‐ protoheme), the 1,3‐C 2 H 3 ‐protoheme (1,3‐ d 6‐protoheme), the 5,8‐C 2 H 3 ‐protoheme (5,8‐ d 6‐protoheme), and the meso‐C 2 H 4 ‐protoheme ( d 4‐protoheme). The entire set of acquired spectra has been analyzed using a deconvolution procedure to help correlate the shifted modes with their counterparts in the spectra of the native forms. Interestingly, modes previously associated with so‐called vinyl bending modes or propionate deformation modes are shown to be quite sensitive to deuteration of the peripheral methyl groups of the macrocycle, shifting by up to 12–15 cm −1 , revealing their complex nature. Of special interest is the fact that shifts observed for the 1,3‐ d 6‐ and 5,8‐ d 6‐protoheme analogues confirm the fact that certain modes are associated with a given portion of the macrocycle; i.e., only certain modes shift upon deuteration of the 1 and 3 methyl groups, while others shift upon deuteration of the 5 and 8 methyl groups. Compared with the spectra previously reported for the corresponding myoglobin derivatives, the data reported here reveal the appearance of several additional features that imply splitting of modes associated with the propionate groups or that are indicative of greater distortion of the heme prosthetic groups. © 2006 Wiley Periodicals, Inc. Biopolymers 83: 455–466, 2006 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com