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J Biol Chem, Vol. 273, Issue 30, 19198-19206, July 24, 1998

Fast-reacting Thiols in Rat Hemoglobins Can Intercept Damaging Species in Erythrocytes More Efficiently Than Glutathione

Ranieri RossiDagger , Donatella Barra§, Andrea Bellelli§, Giovanna Boumis§, Silvia Canofeni§, Paolo Di SimplicioDagger , Lorenzo LusiniDagger , Stefano Pascarella§, and Gino Amiconi§

From the Dagger  Istituto di Clinica delle Malattie Nervose e Mentali, Sezione di Farmacologia, Università di Siena, 53100 Siena, the § Dipartimento di Scienze Biochimiche" A. Rossi Fanelli," Università "La Sapienza," 00185 Roma, and Centro di Biologia Molecolare, CNR, 00185 Roma, Italy

The S-conjugation rates of the free-reacting thiols present on each component of rat hemoglobin with 5,5-dithio-bis(2,2-nitrobenzoic acid) (DTNB) have been studied under a variety of conditions. On the basis of their reactivity with DTNB (0.5 mM), three classes of thiols have been defined as follows: fast reacting (fHbSH), with t1/2 <100 ms; slow reacting (sHbSH), with t1/2 30-50 s; and very slow reacting (vsHbSH), with t1/2 180-270 s. Under paraphysiological conditions, fHbSH (identified with Cys-125beta (H3)) conjugates with DTNB 100 times faster than glutathione and ~4000 times more rapidly than (v)sHbSH (Cys-13alpha (A11) and Cys-93beta (F9)). Such characteristics of fHbSH reactivity that are independent of the quaternary state of hemoglobin are mainly due to the following: (i) its low pK (~6.9, the cysteinyl anion being stabilized by a hydrogen bond with Ser-123beta (H1)) and (ii) the large exposure to the solvent (as measured by analysis of a model of the molecular surface) and make these thiols the kinetically preferred groups in rat erythrocytes for S-conjugation. In addition, because of the high cellular concentration (8 mM, i.e. four times that of glutathione), fHbSHs are expected to intercept damaging species in erythrocytes more efficiently than glutathione, thus adding a new physiopathological role (direct involvement in cellular strategies of antioxidant defense) to cysteinyl residues in proteins.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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