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Title: Heme orientational disorder in human adult hemoglobin reconstituted with a ring fluorinated heme and its functional consequences

Abstract

A ring fluorinated heme, 13,17-bis(2-carboxylatoethyl)-3,8-diethyl-2-fluoro-7,12, 18-trimethyl-porphyrin-atoiron(III), has been incorporated into human adult hemoglobin (Hb A). The heme orientational disorder in the individual subunits of the protein has been readily characterized using {sup 19}F NMR and the O{sub 2} binding properties of the protein have been evaluated through the oxygen equilibrium analysis. The equilibrated orientations of hemes in {alpha}- and {beta}- subunits of the reconstituted protein were found to be almost completely opposite to each other, and hence were largely different from those of the native and the previously reported reconstituted proteins [T. Jue, G.N. La Mar, Heme orientational heterogeneity in deuterohemin-reconstituted horse and human hemoglobin characterized by proton nuclear magnetic resonance spectroscopy, Biochem. Biophys. Res. Commun. 119 (1984) 640-645]. Despite the large difference in the degree of the heme orientational disorder in the subunits of the proteins, the O{sub 2} affinity and the cooperativity of the protein reconstituted with 2-MF were similar to those of the proteins reconstituted with a series of hemes chemically modified at the heme 3- and 8-positions [K. Kawabe, K. Imaizumi, Z. Yoshida, K. Imai, I. Tyuma, Studies on reconstituted myoglobins and hemoglobins II. Role of the heme side chains in the oxygenation of hemoglobin, J.more » Biochem. 92 (1982) 1713-1722], whose O{sub 2} affinity and cooperativity were higher and lower, respectively, relative to those of native protein. These results indicated that the heme orientational disorder could exert little effect, if any, on the O{sub 2} affinity properties of Hb A. This finding provides new insights into structure-function relationship of Hb A.« less

Authors:
 [1];  [1];  [1];  [2];  [3];  [4]
  1. Department of Chemistry, University of Tsukuba, Tsukuba 305-8571 (Japan)
  2. Department of Frontier Sciences, Faculty of Engineering, Hosei University, Koganei, Tokyo 184-8584 (Japan)
  3. Department of Materials Engineering, Nagaoka College of Technology, Nagaoka 940-8532 (Japan)
  4. Department of Chemistry, University of Tsukuba, Tsukuba 305-8571 (Japan). E-mail: yamamoto@chem.tsukuba.ac.jp
Publication Date:
OSTI Identifier:
20979830
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 354; Journal Issue: 3; Other Information: DOI: 10.1016/j.bbrc.2007.01.010; PII: S0006-291X(07)00040-X; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; AFFINITY; ELECTRONIC STRUCTURE; FLUORINE 19; HEME; HEMOGLOBIN; HORSES; MYOGLOBIN; NUCLEAR MAGNETIC RESONANCE; OXYGEN; PARAMAGNETISM; STRUCTURE FUNCTIONS

Citation Formats

Nagao, Satoshi, Hirai, Yueki, Kawano, Shin, Imai, Kiyohiro, Suzuki, Akihiro, and Yamamoto, Yasuhiko. Heme orientational disorder in human adult hemoglobin reconstituted with a ring fluorinated heme and its functional consequences. United States: N. p., 2007. Web. doi:10.1016/j.bbrc.2007.01.010.
Nagao, Satoshi, Hirai, Yueki, Kawano, Shin, Imai, Kiyohiro, Suzuki, Akihiro, & Yamamoto, Yasuhiko. Heme orientational disorder in human adult hemoglobin reconstituted with a ring fluorinated heme and its functional consequences. United States. doi:10.1016/j.bbrc.2007.01.010.
Nagao, Satoshi, Hirai, Yueki, Kawano, Shin, Imai, Kiyohiro, Suzuki, Akihiro, and Yamamoto, Yasuhiko. Fri . "Heme orientational disorder in human adult hemoglobin reconstituted with a ring fluorinated heme and its functional consequences". United States. doi:10.1016/j.bbrc.2007.01.010.
@article{osti_20979830,
title = {Heme orientational disorder in human adult hemoglobin reconstituted with a ring fluorinated heme and its functional consequences},
author = {Nagao, Satoshi and Hirai, Yueki and Kawano, Shin and Imai, Kiyohiro and Suzuki, Akihiro and Yamamoto, Yasuhiko},
abstractNote = {A ring fluorinated heme, 13,17-bis(2-carboxylatoethyl)-3,8-diethyl-2-fluoro-7,12, 18-trimethyl-porphyrin-atoiron(III), has been incorporated into human adult hemoglobin (Hb A). The heme orientational disorder in the individual subunits of the protein has been readily characterized using {sup 19}F NMR and the O{sub 2} binding properties of the protein have been evaluated through the oxygen equilibrium analysis. The equilibrated orientations of hemes in {alpha}- and {beta}- subunits of the reconstituted protein were found to be almost completely opposite to each other, and hence were largely different from those of the native and the previously reported reconstituted proteins [T. Jue, G.N. La Mar, Heme orientational heterogeneity in deuterohemin-reconstituted horse and human hemoglobin characterized by proton nuclear magnetic resonance spectroscopy, Biochem. Biophys. Res. Commun. 119 (1984) 640-645]. Despite the large difference in the degree of the heme orientational disorder in the subunits of the proteins, the O{sub 2} affinity and the cooperativity of the protein reconstituted with 2-MF were similar to those of the proteins reconstituted with a series of hemes chemically modified at the heme 3- and 8-positions [K. Kawabe, K. Imaizumi, Z. Yoshida, K. Imai, I. Tyuma, Studies on reconstituted myoglobins and hemoglobins II. Role of the heme side chains in the oxygenation of hemoglobin, J. Biochem. 92 (1982) 1713-1722], whose O{sub 2} affinity and cooperativity were higher and lower, respectively, relative to those of native protein. These results indicated that the heme orientational disorder could exert little effect, if any, on the O{sub 2} affinity properties of Hb A. This finding provides new insights into structure-function relationship of Hb A.},
doi = {10.1016/j.bbrc.2007.01.010},
journal = {Biochemical and Biophysical Research Communications},
number = 3,
volume = 354,
place = {United States},
year = {Fri Mar 16 00:00:00 EDT 2007},
month = {Fri Mar 16 00:00:00 EDT 2007}
}