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(Received for publication, November 28, 1995, and in revised form, May 2, 1996)
From the Medical Nobel Institute for Biochemistry, Department of
Medical Biochemistry and Biophysics, Karolinska Institutet, S-171
77 Stockholm, Sweden
In activated human neutrophils a burst of nitric
oxide (NO) converts intracellular GSH to
S-nitrosoglutathione (GSNO) which is subsequently cleaved
to restore GSH by an unknown mechanism. We discovered that GSNO is an
NADPH oxidizing substrate for human or calf thymus thioredoxin
reductase (TR) with an apparent Km value of 60 µM and a Kcat of 0.6 × s
Volume 271, Number 32,
Issue of August 9, 1996
pp. 19180-19185
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
1. Addition of human thioredoxin (Trx) stimulated the
initial NADPH oxidation rate severalfold but was accompanied by
progressive inactivation of TR. Escherichia coli TR lacked
activity with GSNO, but with E. coli Trx present, GSNO was
reduced without inhibition of the enzyme. Chemically reduced E. coli Trx-(SH)2 was oxidized to Trx-S2 by
GSNO with a rate constant of 760 M1s1 (7-fold faster than by
GSSG) as measured by tryptophan fluorescence. Analysis of this reaction
in the presence of oxymyoglobin revealed quantitative formation of
metmyoglobin indicative of NO
release. Analysis of GSNO
reduction demonstrated that oxidation of NADPH produced a
stoichiometric amount of free GSH. These results demonstrate a
homolytic cleavage mechanism of GSNO, giving rise to GSH and
NO. GSNO efficiently inhibited the protein disulfide reductase
activity of the complete human or calf thymus thioredoxin systems. Our
results demonstrate enzymatic cleavage of GSNO by TR or Trx and suggest
novel mechanisms for redox signaling.
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