Absence of ligand binding-induced tertiary changes in the multimeric earthworm Lumbricus terrestris hemoglobin a resonance raman study

Gediminas J A Vidugiris, John P. Harrington, Joel M. Friedman, Rhode Elison Hirsch

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

In venebrate hemoglobins, changes in protein tertiary structure induced by either ligand binding or changes in quaternary state are manifested at the heme as reflected in resonance Raman spectral changes involving the iron-proximal histidine stretching mode. No such changes are observed for Lumbricus terreatris hemoglobin. The iron-histidine stretching mode and the porphyrin breathing motion in the deoxy-, oxy-, or CO-photodissociated forms of Lumbricus hemoglobin and human hemoglobin A (pH 7.O and 9.2, the latter to effect Lumbricus hemoglobin subunit dissociation) were studied using pulsed (10 ns) light at 435 nm. In contrast to that observed for hemoglobin A, a comparison of the spectra of the deoxy and photoproduct forms of Lumbricus hemoglobin reveal minimal differences in the region of the iron-histidine and the π electron distribution in the heme moiety. The spectral frequencies are similar to that observed in R-state vertebrate hemoglobins. Such average behavior of the ∼192 hemes present in Lumbricus hemoglobin is more analogous to the Raman spectral properties observed in myoglobin.

Original languageEnglish (US)
Pages (from-to)26190-26192
Number of pages3
JournalJournal of Biological Chemistry
Volume268
Issue number35
StatePublished - Dec 15 1993

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Oligochaeta
Hemoglobins
Ligands
Heme
Histidine
Hemoglobin A
Iron
Stretching
Hemoglobin Subunits
Myoglobin
Porphyrins
Carbon Monoxide
Tertiary Protein Structure
Vertebrates
Respiration
Electrons
Light
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Absence of ligand binding-induced tertiary changes in the multimeric earthworm Lumbricus terrestris hemoglobin a resonance raman study. / Vidugiris, Gediminas J A; Harrington, John P.; Friedman, Joel M.; Hirsch, Rhode Elison.

In: Journal of Biological Chemistry, Vol. 268, No. 35, 15.12.1993, p. 26190-26192.

Research output: Contribution to journalArticle

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AU - Hirsch, Rhode Elison

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