Resonance Raman spectroscopic studies of hydroperoxo derivatives of cobalt-substituted myoglobin.

Journal of Inorganic Biochemistry
Piotr J Mak, James R Kincaid

Abstract

Recent progress in generating and stabilizing reactive heme protein enzymatic intermediates by cryoradiolytic reduction has prompted application of a range of spectroscopic approaches to effectively interrogate these species. The impressive potential of resonance Raman spectroscopy for characterizing such samples has been recently demonstrated in a number of studies of peroxo- and hydroperoxo-intermediates. While it is anticipated that this approach can be productively applied to the wide range of heme proteins whose reaction cycles naturally involve these peroxo- and hydroperoxo-intermediates, one limitation that sometimes arises is the lack of enhancement of the key intraligand nu(O-O) stretching mode in the native systems. The present work was undertaken to explore the utility of cobalt substitution to enhance both the nu(Co-O) and nu(O-O) modes of the CoOOH fragments of hydroperoxo forms of heme proteins bearing a trans-axial histidine linkage. Thus, having recently completed RR studies of hydroperoxo myoglobin, attention is now turned to its cobalt-substituted analogue. Spectra are acquired for samples prepared with (16)O(2) and (18)O(2) to reveal the nu(M-O) and nu(O-O) modes, the latter indeed being observed only for the...Continue Reading

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Citations

Oct 7, 2009·Proceedings of the National Academy of Sciences of the United States of America·Ariel Lewis-BallesterSyun-Ru Yeh
Aug 6, 2010·Biochimica Et Biophysica Acta·Ilia G Denisov, Stephen G Sligar

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