Resonance raman studies of heme structural differences in subunits of deoxy hemoglobin. Biopolymers 2000;57(4):201-7
Date
06/22/2000Pubmed ID
10861384DOI
10.1002/1097-0282(2000)57:4<201::AID-BIP1>3.0.CO;2-7Scopus ID
2-s2.0-0034045353 (requires institutional sign-in at Scopus site) 21 CitationsAbstract
Low frequency resonance Raman (RR) spectra are reported for deoxy hemoglobin (Hb), its isolated subunits, its analogue bearing methine-deuterated hemes in all four subunits (Hb-d(4)), and the hybrids bearing the deuterated heme in only one type of subunit, which are [alpha(d4)beta(h4)](2) and [alpha(h4)beta(d4)](2). Analyzed collectively, the spectra reveal subunit-specific modes that conclusively document subtle differences in structure for the heme prosthetic groups in the two types of subunits within the intact tetramer. Not surprisingly, the most significant spectral differences are observed in the gamma(7) mode that has a major contribution from out of plane bending of the methine carbons, a distortion that is believed to relieve strain in the high-spin heme prosthetic groups. The results provide convincing evidence for the utility of selectively labeled hemoglobin hybrids in unraveling the separate subunit contributions to the RR spectra of Hb and its various derivatives and for thereby detecting slight structural differences in the subunits.
Author List
Podstawka E, Rajani C, Kincaid JR, Proniewicz LMAuthor
James Kincaid PhD Department Chair and Professor, Biophysical Chemistry in the Chemistry department at Marquette UniversityMESH terms used to index this publication - Major topics in bold
DeuteriumHeme
Hemin
Hemoglobins
Humans
Protein Structure, Quaternary
Spectrum Analysis, Raman