S-nitrosation of serum albumin by dinitrosyl-iron complex

Boese, Matthias; Mordvintcev, Peter I.; Vanin, Anatoly F.; Busse, Rudi; Mülsch, Alexander

doi:10.1074/jbc.270.49.29244

Cited by 259Nitric Oxide and Endothelin EffectsHemoglobin structure and functionRedox biology and oxidative stress

S-nitrosation of serum albumin by dinitrosyl-iron complex

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Boese, Matthias, Mordvintcev, Peter I., Vanin, Anatoly F., Busse, Rudi, Mülsch, Alexander·1995·Journal of Biological Chemistry

DOI 10.1074/jbc.270.49.29244

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Abstract

The objective of this study was to identify a potential mechanism for S-nitrosation of proteins. Therefore, we assessed S-nitrosation of bovine serum albumin by dinitrosyl-iron-di-L-cysteine complex [(NO)2Fe(L-cysteine)2], a compound similar to naturally occurring iron-nitrosyls. Within 5-10 min, (NO)2Fe(L-cysteine)2 generated paramagnetic albumin-bound dinitrosyl-iron complex and S-nitrosoalbumin in a ratio of 4:1. Although S-nitroso-L-cysteine was concomitantly formed in low amounts, its concentration was not sufficient to account for formation of S-nitrosoalbumin via a trans-S-nitrosation reaction. Low oxygen tension did not affect S-nitrosation by the dinitrosyl-iron complex thus excluding the involvement of oxygenated NOx-species in the nitrosation reaction. Blockade of albumin histidine residues by pyrocarbonate, which prevented formation of dinitrosyl-iron-albumin complex, did not inhibit S-nitrosation of albumin. Thus, S-nitrosation of albumin by (NO)2Fe(L-cysteine)2 can proceed by direct attack of a nitrosyl moiety on the protein thiolate, without previous binding of the iron. We conclude that protein-bound dinitrosyl-iron complexes detected in high concentrations in certain tissues provide a reservoir of S-nitrosating species, e.g. low molecular dinitrosyl iron complexes.

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DNICs can be prepared from S-nitrosothiols, suggesting that NO+ transfer from RSNO to iron occurs readily.
“That they can be prepared from S-nitrosothiols [105] suggests that NO + transfer from RSNO to iron occurs readily.”
From On the chemical biology of the nitrite/sulfide interaction (2015) · cites this paper as [105]

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Self-citation

Authors: Boese, M., Mordvintcev, P. I., Vanin, A. F., Busse, R., & Mülsch, A.
Affiliations: Goethe University Frankfurt (DE)
Corresponding author: Mülsch, Alexander
ORCID: Vanin, Anatoly F.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1995-12
Volume: 270
Issue: 49
Pages: 29244-29249
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.270.49.29244
OpenAlex: W1977448081
Cited by: 259
References: 40
Citations by year: 2026: 1 · 2025: 3 · 2024: 5 · 2023: 5 · 2022: 7 · 2021: 13 · 2020: 5 · 2019: 9 · 2018: 6 · 2017: 5 · 2016: 7 · 2015: 4 · 2014: 9 · 2013: 10 · 2012: 8
FWCI: 4.99
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 9108 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: S-nitrosylation, bovine serum albumin, dinitrosyl iron complexes, S-nitroso-L-cysteine, histidine residues, oxygen partial pressure, nitric oxide
MeSH terms: Animals, Cattle, Cysteine, Oxygen, Serum Albumin, Bovine

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S-nitrosation of serum albumin by dinitrosyl-iron complex

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