ArticleJournal of fluorescence2008
Oxygen-dependent oxidation of Fe(II) to Fe(III) and interaction of Fe(III) with bovine serum albumin, leading to a hysteretic effect on the fluorescence of bovine serum albumin.
Article in Journal of fluorescence, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed, 44 citations in OpenAlex.
- Modulation of pulsed electric field induced oxidative processes in protein solutions by pro- and antioxidants sensed by biochemiluminescence.Scientific reports · 2024Article
- Influence of aluminum and iron chlorides on the parameters of zigzag patterns on films dried from BSA solutions.Scientific reports · 2023Article
- A Metal-Ion-Incorporated Mussel-Inspired Poly(Vinyl Alcohol)-Based Polymer Coating Offers Improved Antibacterial Activity and Cellular Mechanoresponse Manipulation.Angewandte Chemie (International ed. in English) · 2022Article
- The (Bio)Chemistry of Non-Transferrin-Bound Iron.Molecules (Basel, Switzerland) · 2022Review
- Difference in the binding mechanism of distinct antimony forms in bovine serum albumin.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2021Article
- Modification of human serum albumin under induced oxidation.Doklady. Biochemistry and biophysics · 2017Article
- Complex Nature of Protein Carbonylation Specificity After Metal-Catalyzed Oxidation.Pharmaceutical research · 2017Article
- The Spectroscopy Study of the Binding of an Active Ingredient of Dioscorea Species with Bovine Serum Albumin with or without Co(2+) or Zn(2+).Evidence-based complementary and alternative medicine : eCAM · 2014Article
- The binding characteristics of isoniazid with copper-zinc superoxide dismutase and its effect on enzymatic activity.Chemistry Central journal · 2013Article
- Expression of virulence factors by Staphylococcus aureus grown in serum.Applied and environmental microbiology · 2011Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The serum albumin is the most abundant protein in blood plasma and the iron is essential for many cellular processes. However, the interaction between Fe(3+) and haem-free serum albumin remains unclear. Here we provide evidence for the fact that haem-free BSA possesses one specific Fe(3+)-binding site. The binding of Fe(3+) to BSA results in a significant quenching of the Trp fluorescence of BSA. The average apparent dissociation constant value for the interaction of Fe(3+) and BSA is 3.46 x 10(-8)+/-3 x 10(-10) M at 37 degrees C and 3.30 x 10(-8)+/-5 x 10(-10) M at 25 degrees C, respectively, as determined by fluorescence titration. Addition of 50 microM Fe(2+) to 1 microM BSA results in an obvious hysteretic effect on the fluorescence of BSA. The time-dependent fluorescence quenching of BSA by Fe(2+) is not caused by the Fe(2+)-induced conformational change of BSA, but the oxygen-dependent oxidation of Fe(2+) to Fe(3+). Fe(2+) undergoes an oxygen-dependent oxidation to Fe(3+) under aerobic conditions, which is accelerated by the interaction of BSA with Fe(3+) and extensively inhibited under anaerobic conditions. The results suggest that BSA may take part in non-transferrin bound iron transfer.
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Registered trials
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