Inhibition of S-nitrosation of reduced glutathione in aerobic solutions of nitric oxide by phosphate and other inorganic anions.

Abstract:

:Reduced glutathione is nitrosated in aerobic solutions of nitric oxide under physiological conditions; however, the extent of S-nitrosation was found to be dependent on the inorganic anions present. Of nine anions tested, the bifunctional anions, arsenate, phosphate, and pyrophosphate (40 mM), inhibited the S-nitrosation reaction from 20 to 40%, whereas SO4(2-), H3BO3, SCN-, NO3-, Cl-, and acetate inhibited this reaction < or = 15%. A mechanism of inhibition is presented that involves the catalytic hydrolysis of N2O3 by the bifunctional anions; however, using [18O]phosphate as inhibitor, only 10% of the theoretically produced N2O3 was found to be hydrolyzed to nitrite via this mechanism as calculated from the loss of 18O from phosphate. We conclude that this mechanism accounts for only a minor part of the increased inhibition of S-nitrosation by these bifunctional anions.

journal_name

Biochem Pharmacol

journal_title

Biochemical pharmacology

authors

DeMaster EG,Quast BJ,Mitchell RA

doi

10.1016/s0006-2952(96)00825-8

subject

Has Abstract

pub_date

1997-02-21 00:00:00

pages

581-5

issue

4

eissn

0006-2952

issn

1873-2968

pii

S0006295296008258

journal_volume

53

pub_type

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