Binding of monovalent anions to human serum transferrin

Harris, Wesley R.; Cafferty, Anne M.; Abdollahi, Sohrab; Trankler, Kevin A.

doi:10.1016/s0167-4838(97)00152-0

Cited by 34 publications

(30 citation statements)

References 39 publications

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“…The binding of nonsynergistic anions to apo-hTF probably interferes with metal binding by competing directly with the binding of the synergistic anion. 102 Competition experiments have shown that the strength of nonsynergistic anion binding to transferrin follows the order HPO 4 2 > SO 4 2-= F -> ClO 4 -= Cl -= Br -. Titration of anions with apo-transferrin leads to negative absorption bands centered at 245 and 290 nm in the difference UV spectra, which are remarkably similar to those produced by the binding of metal ions to apo-transferrin.…”

Section: A Strength Of Metal and Anion Bindingmentioning

confidence: 99%

Transferrin as a Metal Ion Mediator

1999

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Hongzhe Sun (left) was born in Luoyang, the ancient capital of China, and received his B.Sc. and M.Sc. degrees form the Chinese Academy of Sciences in 1985 and 1990. He then became a research associate and lecturer at Nanjing University in China. In 1996 he obtained his Ph.D. from the University of London, working on the biological chemistry of bismuth drugs with Peter Sadler. After 2 years at the University of Edinburgh as a GlaxoWellcome Research Fellow, he took a position as an Assistant Professor in the Department of Chemistry at the University of Hong Kong in 1998. His current research interests are in the areas of biological inorganic chemistry and NMR spectroscopy.Hongyan Li (middle) was born in north China,

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Section: A Strength Of Metal and Anion Bindingmentioning

confidence: 99%

Transferrin as a Metal Ion Mediator

1999

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“…doi:10.1016/j.jinorgbio.2004.08.008 protein. Bicarbonate will bind weakly to apotransferrin in the absence of iron [11][12][13]. However, the carbonate is so critical to metal binding, that virtually no iron will bind to apotransferrin in the absence of bicarbonate or a suitable substitute anion [14,15].…”

Section: Introductionmentioning

confidence: 99%

Release of iron from transferrin by phosphonocarboxylate and diphosphonate chelating agents

Harris

Brook

Spilling

et al. 2004

Journal of Inorganic Biochemistry

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“…Anions bind strongly but differentially to both the lobes of the apo structure of transferrins (5,(37)(38)(39)(40). With respect to the synergistic anion-binding site, a second class of anion-binding sites was proposed to be involved in inducing the conformational change, which is the rate-limiting step in the iron release pathway proposed by Bates and coworkers (27,28).…”

Section: Discussionmentioning

confidence: 99%

Anion-mediated Iron Release from Transferrins

Muralidhara¹,

Hirose

2000

Journal of Biological Chemistry

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Iron release process of ovotransferrin N-lobe (N-oTf) to anion/chelators has been resolved using kinetic and mechanistic approach. The iron release kinetics of N-oTf were measured at the endosomal pH of 5.6 with three different anions such as nitrilotriacetate, pyrophosphate, and sulfate using stopped flow spectrofluorimetric method, all yielding clear biphasic progress curves. The two observed rate constants and the corresponding amplitudes obtained from the double exponential curve fit to the biphasic curves varied depending on the type and concentration of anions. Several possible models for the iron release kinetic mechanism were examined on the basis of a newly introduced quantitative equation. Results from the curve fitting analyses were consistent with a dual pathway mechanism that includes the competitive iron release from two different protein states, namely, X and Y, with the respective first order rate constants of K 1 and K 2 (X, domain closed holo N-oTf; Y, anion induced different conformer of holo N-oTf). The reversible interconversions of X to Y and Y to X are driven by the second order rate constant k 3 and the first order rate constant K 4 , respectively. The obtained rate constants were greatly variable for the three anions depending on the synergistic or nonsynergistic nature. In the light of the anion-binding sites of N-oTf located crystallographically, the compatible mechanistic model that includes competitive anion binding to the iron coordination sites and to a specific anion site is suggested for the dual pathway iron release mechanism.

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Binding of monovalent anions to human serum transferrin

Cited by 34 publications

References 39 publications

Transferrin as a Metal Ion Mediator

Transferrin as a Metal Ion Mediator

Release of iron from transferrin by phosphonocarboxylate and diphosphonate chelating agents

Anion-mediated Iron Release from Transferrins

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