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Resonance Raman spectroscopic studies in copper reconstituted and hybrid hemoglobins: Probe into subunit heterogeneity
Author(s) -
Swarnalatha V.,
Balakrishnan G.,
Manoharan P. T.
Publication year - 2002
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.10065
Subject(s) - chemistry , copper , raman spectroscopy , electron paramagnetic resonance , resonance raman spectroscopy , resonance (particle physics) , reactivity (psychology) , protein subunit , metal , heme , hemeprotein , spectroscopy , crystallography , inorganic chemistry , nuclear magnetic resonance , biochemistry , organic chemistry , quantum mechanics , medicine , physics , alternative medicine , particle physics , pathology , optics , gene , enzyme
Copper reconstituted hemoglobin (CuHb), copper containing T‐state hybrid hemoglobins like α 2 (Ni)β 2 (Cu), and α 2 (Cu)β 2 (Ni), and intermediate R‐state hybrids like α 2 (CO‐Fe)β 2 (Cu) and α 2 (Cu)β 2 (Fe‐CO) are studied using resonance Raman (RR) spectroscopy at two different excitation wavelengths. The high frequency RR region in CuHb indicates the presence of both 4‐ and 5‐coordinate forms of Cu(II). In hybrid Hbs, the presence of two distinct metal ion environments within one particular subunit is evident. This is also consistent with previous findings using EPR spectroscopy and sulfydryl reactivity studies on these hybrid Hbs. The low frequency RR region on these copper derivatives of HbA further suggests the existence of two different heme moieties within the subunit. © 2002 Wiley Periodicals, Inc. Biopolymers (Biospectroscopy) 67: 156–166, 2002