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S-Nitrosation of Serum Albumin by Dinitrosyl-Iron Complex
Open accessAbstract
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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“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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Metadata
- 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)
- 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
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › 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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