Faculty Collaboration Database

Resonance raman studies of heme structural differences in subunits of deoxy hemoglobin. Biopolymers 2000;57(4):201-7

Date

06/22/2000

Pubmed ID

10861384

DOI

10.1002/1097-0282(2000)57:4<201::AID-BIP1>3.0.CO;2-7

Scopus ID

2-s2.0-0034045353 (requires institutional sign-in at Scopus site)   22 Citations

Abstract

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 LM

Author

James Kincaid PhD Department Chair and Professor, Biophysical Chemistry in the Chemistry department at Marquette University

MESH terms used to index this publication - Major topics in bold

Deuterium
Heme
Hemin
Hemoglobins
Humans
Protein Structure, Quaternary
Spectrum Analysis, Raman