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JBC, Vol. 253, Issue 23, 8433-8443, Dec, 1978
P. A. Craven and F. R. DeRubertis
Purification of soluble guanylate cyclase activity from rat liver resulted
in loss of enzyme responsiveness to N-methyl-N'-nitro-N-nitrosoguanidine
(MNNG), nitroprusside, nitrite, and NO. Responses were restored by addition
of heat-treated hepatic supernatant fraction, implying a requirement for
heat-stable soluble factor(s) in the optimal expression of the actions of
the activators. Addition of free hematin, hemoglobin, methemoglobin, active
or heat-inactivated catalase partially restores responsiveness of purified
guanylate cyclase to MNNG, NO, nitrite, and nitroprusside. These responses
were markedly potentiated by the presence of an appropriate concentration
of reducing agent (dithiothreitol, ascorbate, cysteine, or glutathione),
which maintains heme iron in the ferro form and favors formation of
paramagnetic nitrosyl . heme complexes from the activators. High
concentrations of heme or reducing agents were inhibitory, and heme was not
required for the expression of the stimulatory effects of Mn2+ or Mg2+ on
purified guanylate cyclase. Preformed nitrosyl hemoglobin (10 micron)
increased activity of the purified enzyme 10- to 20-fold over basal with
Mn2+ as the metal cofactor and 90- to 100-fold with Mg2+. Purified
guanylate cyclase was more sensitive to preformed NO-hemoglobin (minimally
effective concentration, 0.1 micron) than to MNNG (1 micron), nitroprusside
(50 micron), or nitrite (1 mM). A reducing agent was not required for
optimal stimulation of guanylate cyclase by NO-hemoglobin. Maximal
NO-hemoglobin-responsive guanylate cyclase was not further increased by
subsequent addition of NO, MNNG, nitrite, or nitroprusside. Activation by
each agent resulted in analogous alterations in the Mn2+ and Mg2+
requirements of enzyme activity, and responses were inhibited by the
thiol-blocking agents N-ethylmaleimide, arsenite, or iodoacetamide. The
results suggest that NO-hemoglobin, MNNG, NO, nitrite, and nitroprusside
activate guanylate cyclase through similar mechanisms. The stimulatory
effects of preformed NO-hemoglobin combined with the clear requirements for
heme plus a reducing agent in the optimal expression of the actions of
MNNG, NO, and related agents are consistent with a role for the
paramagnetic nitrosyl . heme complex in the activation of guanylate
cyclase.
Restoration of the responsiveness of purified guanylate cyclase to nitrosoguanidine, nitric oxide, and related activators by heme and hemeproteins. Evidence for involvement of the paramagnetic nitrosyl-heme complex in enzyme activation
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