Reactions of sulfur-nitrosyl iron complexes of “g=2.03” family with hemoglobin (Hb): Kinetics of Hb–NO formation in aqueous solutions

Санина, Н. А.; Syrtsova, L. A.; Shkondina, N. I.; Rudneva, T. N.; Malkova, E. S.; Bazanov, T. A.; Котельников, А. И.; Алдошин, С. М.

doi:10.1016/j.niox.2006.10.005

Cited by 49 publications

(54 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Unlike nitro esters and other syn thetic (organic and inorganic) NO donors, the nitrosyl [1Fe-S] and [2Fe-2S] complexes generate NO without activation: due to hydrolysis in a protic medium. 1 These compounds have been synthesized 2-5 for the first time at the Institute of Chemical Physics, Russian Academy of Sciences. They are models of active centers of the nitrosyl [1Fe-2S] and [2Fe-2S] proteins, which are unique "de pots" of endogenic NO.…”

mentioning

confidence: 99%

Hemoglobin-stabilized tetranitrosyl binuclear iron complex with pyridine-2-yl in aqueous solutions

et al. 2007

View full text Add to dashboard Cite

The tetranitrosyl iron complex with pyridin 2 yl [Fe 2 (SC 5 H 4 N) 2 (NO) 4 ] (1) has higher NO donating activity in 3% aqueous solutions of DMSO (pH 7.0, 25 °C) than the organic NO donor, viz., adduct of NO with diethylenetriamine (NO adduct). The NO concentration was determined by the spectrophotometric method based on the formation of an NO complex with hemoglobin (Hb). The apparent first order rate constants of the studied reactions are (6.15±0.6)•10 -1 s -1 and (0.8±0.08)•10 -1 s -1 for complex 1 and the NO adduct, respectively, at an Hb concentration of 2•10 -1 mol L -1 and the ratio [NO donor]/[Hb] = 10. The effect of Hb and [NO donor]/[Hb] ratio on the rate of NO generation from a solution of complex 1 was studied. For a fourfold decrease in the concentration of complex 1 the reaction rate constant decreases to 0.5•10 -4 s -1 , whereas the fourfold increase in the Hb concentration results in the stabilization of complex 1.

show abstract

mentioning

confidence: 99%

Hemoglobin-stabilized tetranitrosyl binuclear iron complex with pyridine-2-yl in aqueous solutions

et al. 2007

View full text Add to dashboard Cite

show abstract

“…This evidences that only Hb and HbNO contribute to the absorption spectrum, as in the case of the iron nitrosyl complexes of this class studied earlier. 13 The kinetics of HbNO accumulation was first deter mine by processing of the absorption spectra (see for studying the kinetics of formation of NO generated by complex 1 in aqueous solutions in the presence of Hb.…”

Section: Resultsmentioning

confidence: 99%

“…13 The data on the kinetics of HbNO formation in the presence of complex 1 (Fig. 4) were obtained by the analy sis of the absorption spectra (see Fig.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Formation of nitrosothiols by the reaction of different forms of hemoglobin with (tetranitrosyl)bis(pyrimidin-2-ylthio)diiron

et al. 2009

View full text Add to dashboard Cite

The reaction of hemoglobin (Hb), oxyhemoglobin (HbO 2 ), and methemoglobin (metHb) with the tetranitrosyl iron complex of the μ 2 S type [Fe 2 (SC 4 H 3 N 2 ) 2 (NO) 4 ] (1) was studied. The reaction results in the nitrosylation of the free SH group of 93 β cysteine in these forms of hemoglobin. The change in the Hb, HbO 2 , and metHb concentrations was monitored by spectrophotometry, recording the difference absorption spectra of the experimental systems with these forms of hemoglobin and the buffer containing complex 1 in the same concentra tion. The absorption spectra were processed to obtain the components using the MATHCAD method. The nitrosothiol concentration was determined by the Saville reaction. In a protic medium containing 3.3% DMSO, complex 1 spontaneously generates NO due to hydrolysis (k = 3.7•10 -4 s -1 ). Oxyhemoglobin reacts with evolved NO to form metHb. Complex 1 reduces metHb with a high rate to yield Hb (k = 6.7•10 -3 s -1 ) followed by the formation of HbNO (k = 6.5•10 -3 s -1 ). Oxidized complex 1 yields NO with a higher rate than the starting complex does. The reaction of HbO 2 and metHb (0.02 mmol L -1 ) with complex 1 affords nitrosothiols in micromolar concentration during 5 min, and no nitrosothiol is formed in the case of Hb.

show abstract

“…These gave a k on value of 1.1 Â 10 9 M À1 s À1 for the reaction equivalent to that described by (10) [26]. Although k on has not been measured for this compound, it has been determined for several similar esters, and k off values of (1-9) Â 10 À3 s À1 were found [105]. Thus, the equilibrium constant for NO dissociation from such RSEs would appear to be about 10 À12 M. Flash photolysis studies of Roussin's black salt anion Fe 4 S 3 (NO) 7 -displayed similar reversible NO photodissociation in aqueous solutions [106].…”

Section: Non-heme Iron Complexesmentioning

confidence: 89%

Mechanisms of Nitric Oxide Reactions Mediated by Biologically Relevant Metal Centers

Ford

Pereira

Miranda

2013

Nitrosyl Complexes in Inorganic Chemistry, Biochemistry and Medicine II

View full text Add to dashboard Cite

show abstract

Reactions of sulfur-nitrosyl iron complexes of “g=2.03” family with hemoglobin (Hb): Kinetics of Hb–NO formation in aqueous solutions

Cited by 49 publications

References 15 publications

Hemoglobin-stabilized tetranitrosyl binuclear iron complex with pyridine-2-yl in aqueous solutions

Hemoglobin-stabilized tetranitrosyl binuclear iron complex with pyridine-2-yl in aqueous solutions

Formation of nitrosothiols by the reaction of different forms of hemoglobin with (tetranitrosyl)bis(pyrimidin-2-ylthio)diiron

Mechanisms of Nitric Oxide Reactions Mediated by Biologically Relevant Metal Centers

Contact Info

Product

Resources

About