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J. Biol. Chem., Vol. 275, Issue 22, 16738-16745, June 2, 2000
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From the § Howard Hughes Medical Institute, the
S-Nitrosohemoglobin (SNO-Hb) is a
vasodilator whose activity is allosterically modulated by oxygen
("thermodyamic linkage"). Blood vessel contractions are favored in
the oxygenated structure, and vasorelaxant activity is "linked" to
deoxygenation, as illustrated herein. We further show that
transnitrosation reactions between SNO-Hb and ambient thiols transduce
the NO-related bioactivity, whereas NO itself is inactive. One
remaining problem is that the amounts of SNO-Hb present in
vivo are so large as to be incompatible with life were all the
S-nitrosothiols transformed into bioactive equivalents
during each arterial-venous cycle. Experiments were therefore
undertaken to address how SNO-Hb conserves its NO-related activity. Our
studies show that 1) increased O2 affinity of SNO-Hb (which
otherwise retains allosteric responsivity) restricts the hypoxia-induced allosteric transition that exchanges NO groups with
ambient thiols for vasorelaxation; 2) some NO groups released from
Cys
Functional Coupling of Oxygen Binding and Vasoactivity in
S-Nitrosohemoglobin*
,
, and§**
Department of Medicine, and the ¶ Nicholas School
for the Environment, Duke University Medical Center, Durham, North
Carolina 27710 and the Department of Chemistry, Montana State
University, Bozeman, Montana 59717
93 upon transition to T structure are autocaptured by
the hemes, even in the presence of glutathione; and 3) an
O2-dependent equilibrium between SNO-Hb and
iron nitrosylhemoglobin acts to conserve NO. Thus, by sequestering a
significant fraction of NO liberated upon transition to T structure, Hb
can conserve NO groups that would otherwise be released in an untimely
or deleterious manner.
*
This work was supported by National Institutes of Health
Grants R01 HL52529-05 and HL59130-02 (to J. S. S.) and Grant K08 HL04014-01 (to T. J. M.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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