Structural and functional properties of hemoglobins from unicellular organisms as revealed by resonance Raman spectroscopy

Tsuyoshi Egawa, Syun Ru Yeh

Research output: Contribution to journalArticlepeer-review

92 Scopus citations

Abstract

Hemoglobins have been discovered in organisms from virtually all kingdoms. Their presence in unicellular organisms suggests that the gene for hemoglobin is very ancient and that the hemoglobins must have functions other than oxygen transport, in view of the fact that O2 delivery is a diffusion-controlled process in these organisms. Based on sequence alignment, three groups of hemoglobins have been characterized in unicellular organisms. The group-one hemoglobins, termed truncated hemoglobins, consist of proteins with 110-140 amino acid residues and a novel two-over-two α-helical sandwich motif. The group-two hemoglobins, termed flavohemoglobins, consist of a hemoglobin domain, with a classical three-over-three α-helical sandwich motif, and a flavin-containing reductase domain that is covalently attached to it. The group-three hemoglobins consist of myoglobin-like proteins that have high sequence homology and structural similarity to the hemoglobin domain of flavohemoglobins. In this review, recent resonance Raman studies of each group of these proteins are presented. Their implications are discussed in the context of the structural and functional properties of these novel hemoglobins.

Original languageEnglish (US)
Pages (from-to)72-96
Number of pages25
JournalJournal of Inorganic Biochemistry
Volume99
Issue number1
DOIs
StatePublished - Jan 2005

Keywords

  • Hemeprotein
  • Hemoglobin
  • Raman
  • Vibrational spectrum

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Fingerprint

Dive into the research topics of 'Structural and functional properties of hemoglobins from unicellular organisms as revealed by resonance Raman spectroscopy'. Together they form a unique fingerprint.

Cite this