TY - JOUR
T1 - Structural and functional properties of hemoglobins from unicellular organisms as revealed by resonance Raman spectroscopy
AU - Egawa, Tsuyoshi
AU - Yeh, Syun Ru
N1 - Funding Information:
This work was supported by the National Institute of Health Research Grant HL65465 to S.-R.Y. We thank Dr. Denis L. Rousseau for many invaluable discussions. We are also grateful to Dr. Jack Peisach for carefully reading the manuscript and the helpful suggestions.
PY - 2005/1
Y1 - 2005/1
N2 - 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.
AB - 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.
KW - Hemeprotein
KW - Hemoglobin
KW - Raman
KW - Vibrational spectrum
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U2 - 10.1016/j.jinorgbio.2004.10.017
DO - 10.1016/j.jinorgbio.2004.10.017
M3 - Article
C2 - 15598493
AN - SCOPUS:10644274523
SN - 0162-0134
VL - 99
SP - 72
EP - 96
JO - Journal of Inorganic Biochemistry
JF - Journal of Inorganic Biochemistry
IS - 1
ER -