ArticleProtein science : a publication of the Protein Society2010
Excited-state lifetime studies of the three tryptophan residues in the N-lobe of human serum transferrin.
Article in Protein science : a publication of the Protein Society, 2010. 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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Who cites it
10 citing papers in PubMed.
- Interactions of Chemically Synthesized Ferrihydrite Nanoparticles with Human Serum Transferrin: Insights from Fluorescence Spectroscopic Studies.International journal of molecular sciences · 2021Article
- Photophysical Studies of a Catechol Based Polyfunctional Dipodal Chelator: Application for Optical Probe for Selective Detection of Fe(III).Journal of fluorescence · 2020Article
- Structural characterization of metal binding to a cold-adapted frataxin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- Iron binding at specific sites within the octameric HbpS protects streptomycetes from iron-mediated oxidative stress.PloS one · 2013Article
- Spectroscopic Study of the Interactions of Ruthenium-Ketoconazole Complexes of Known Antiparasitic Activity with Human Serum Albumin and Apotransferrin.Journal of the Mexican Chemical Society · 2013Article
- 1-Aminocyclopropane-1-carboxylic acid oxidase: insight into cofactor binding from experimental and theoretical studies.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012Article
- The long history of iron in the Universe and in health and disease.Biochimica et biophysica acta · 2012Review
- Dating bloodstains with fluorescence lifetime measurements.Chemistry (Weinheim an der Bergstrasse, Germany) · 2012Article
- Applications of phasor plots to in vitro protein studies.Analytical biochemistry · 2011Article
- Applications of phasors to in vitro time-resolved fluorescence measurements.Analytical biochemistry · 2011Article
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Abstract
The energy transfer from the three Trp residues at positions 8, 128, and 264 within the human serum transferrin (hTF) N-lobe to the ligand to metal charge transfer band has been investigated by monitoring changes in Trp fluorescence emission and lifetimes. The fluorescence emission from hTF N-lobe is dominated by Trp264, as revealed by an 82% decrease in the quantum yield when this Trp residue is absent. Fluorescence lifetimes were determined by multifrequency phase fluorometry of mutants containing one or two Trp residues. Decays of these samples are best described by two or three discrete lifetimes or by a unimodal Lorentzian distribution. The discrete lifetimes and the center of the lifetime distribution for samples containing Trp128 and Trp264 are affected by iron. The distribution width narrows on iron removal and is consistent with a decrease in dynamic mobility of the dominant fluorophore, Trp264. Both the quantum yield and the lifetimes are lower when iron is present, however, not proportionally. The greater effect of iron on quantum yields is indicative of nonexcited state quenching, i.e., static quenching. The results of these experiments provide quantitative data strongly suggesting that Förster resonance energy transfer is not the sole source of Trp quenching in the N-lobe of hTF.
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