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Journal of Biochemistry 2004 136(5):595-600; doi:10.1093/jb/mvh166
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© 2004 The Japanese Biochemical Society

BIOCHEMISTRY

Oxygen Equilibrium and EPR Studies on {alpha}1ß1 Hemoglobin Dimer

Balan Venkatesh1, Gentaro Miyazaki1, Kiyohiro Imai2, Hideki Morimoto1 and Hiroshi Hori1,*

1 Division of Bioengineering, Graduate School of Engineering Science, Osaka University, Toyonaka, Osaka 560-8531; and 2 Department of Materials Chemistry, Faculty of Engineering Hosei University, Koganei, Tokyo 184-8584

We undertook this project to clarify whether hemoglobin (Hb) dimers have a high affinity for oxygen and cooperativity. For this, we prepared stable Hb dimers by introducing the mutation Trp->Glu at ß37 using our Escherichia coli expression system at the {alpha}1ß2 interface of Hb, and analyzed their molecular properties. The mutant hybrid Hbs with a single oxygen binding site were prepared by substituting Mg(II) protoporphyrin for ferrous heme in either the {alpha} or ß subunit, and the oxygen binding properties of the free dimers were investigated. Molecular weight determination of both the deoxy and CO forms showed all these molecules to be dimers in the absence of IHP at different protein concentrations. Oxygen equilibrium measurements showed high affinity and non-cooperative oxygen binding for all mutant Hb and hybrid Hb dimers. However, EPR results on the [{alpha}N(Fe-NO)ßM(Mg)] hybrid showed some {alpha}1ß1 interactions. These results provide some clues as to the properties of Hb dimers, which have not been studied extensively owing to practical difficulties in their preparation.

* To whom correspondence should be addressed. Tel: +81-6-6850-6551, Fax: +81-6-6850-557, E-mail: hori{at}bpe.es.osaka-u.ac.jp


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