Lanthanide ion luminescence probes of biomolecular structure

Horrocks, William DeW.; Albin, Michael; Breen, Patrick J.; Hild, E.; Mulqueen, Paul; Rhee, Moo-Jhong; Sudnick, Daniel R.

doi:10.1016/0022-5088(83)90061-9

Cited by 6 publications

(11 citation statements)

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“…This selectivity is much greater than would be expected on the basis of charge and radius alone (∼10 4 ). 4,86,89 Furthermore, LanM binds early REs with higher affinity than late REs, whereas chelators typically prefer the more Lewis-acidic, late REs. 8 These intriguing and unusual properties have motivated us to study LanM as a model system for determining the rules of highly selective biological lanthanide coordination.…”

Section: Lanthanide Recognition In Cellsmentioning

confidence: 99%

The Chemistry of Lanthanides in Biology: Recent Discoveries, Emerging Principles, and Technological Applications

2019

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The essential biological role of rare earth elements lay hidden until the discovery in 2011 that lanthanides are specifically incorporated into a bacterial methanol dehydrogenase. Only recently has this observation gone from a curiosity to a major research area, with the appreciation for the widespread nature of lanthanide-utilizing organisms in the environment and the discovery of other lanthanide-binding proteins and systems for selective uptake. While seemingly exotic at first glance, biological utilization of lanthanides is very logical from a chemical perspective. The early lanthanides (La, Ce, Pr, Nd) primarily used by biology are abundant in the environment, perform similar chemistry to other biologically useful metals and do so more efficiently due to higher Lewis acidity, and possess sufficiently distinct coordination chemistry to allow for selective uptake, trafficking, and incorporation into enzymes. Indeed, recent advances in the field illustrate clear analogies with the biological coordination chemistry of other metals, particularly CaII and FeIII, but with unique twists—including cooperative metal binding to magnify the effects of small ionic radius differences—enabling selectivity. This Outlook summarizes the recent developments in this young but rapidly expanding field and looks forward to potential future discoveries, emphasizing continuity with principles of bioinorganic chemistry established by studies of other metals. We also highlight how a more thorough understanding of the central chemical question—selective lanthanide recognition in biology—may impact the challenging problems of sensing, capture, recycling, and separations of rare earths.

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Section: Lanthanide Recognition In Cellsmentioning

confidence: 99%

The Chemistry of Lanthanides in Biology: Recent Discoveries, Emerging Principles, and Technological Applications

2019

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“…We also probed calcium-binding using another calcium probe, terbium. The ionic radius of terbium is similar to that of calcium, thus making it an ideal choice for use as a calcium mimic probe [31]. Terbium ions bind to the calcium-binding sites in proteins and induce luminescence peaks at 492 nm and 547 nm via energy transfer from Trp and Tyr residues [32].…”

Section: Probing Calcium-binding By Terbiummentioning

confidence: 99%

“…bB2-and bA3-crystallins presaturated with calcium showed increased fluorescence intensity upon adding increasing concentrations of terbium, which indicated that terbium displaced the bound calcium. This is expected because terbium ions have a higher affinity All lens b-crystallins are calcium-binding proteins than calcium for calcium-binding sites in the protein due to the higher positive charge of terbium than calcium [31].…”

Section: Probing Calcium-binding By Terbiummentioning

confidence: 99%

“…We, therefore, carried out terbium binding to this crystallin by ITC and determined the binding constant for the calcium mimic probe. Terbium is believed to bind strongly to calcium-binding sites of proteins compared to calcium due to its higher charge ratio than calcium, even though both ions have similar ionic radii [31]. The dissociation constants of terbium-binding to bA3crystallin range from 2.7 mm to 40 lm ( Table 1).…”

Section: Calcium-binding By Isothermal Titration Calorimetrymentioning

confidence: 99%

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Calcium‐binding to lens βB2‐ and βA3‐crystallins suggests that all β‐crystallins are calcium‐binding proteins

Jobby

Sharma

2007

The FEBS Journal

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Crystallins are abundant proteins found in the eye lens of vertebrates that belong to two superfamilies named as a-crystallins and bc-crystallins [1]. a-Crystallins are known to play an important role as molecular chaperone [2]. On the other hand, bc-crystallins are thought to play structural role in the mammalian eye lens. Their nonstructural functions, which appear to be very important, have not been elucidated [3].b-Crystallins from vertebrate eye lens are a group of seven proteins broadly classified into four acidic (bA1 ⁄ A3, bA2 and bA4) and three basic b-crystallins (bB1, bB2, and bB3). b-Crystallins have high sequence similarity and identity [4]. Acidic b-crystallins have both N-and C-terminal extensions, whereas basic b-crystallins have only N-terminal extensions. All b-crystallins have four Greek key motifs organized into two crystallin domains. In this respect, b-crystallins are similar to c-crystallins, which also have a similar domain organization and structure [5,6]. The major difference between the b-and c-crystallins is their oligomeric state. c-Crystallins are monomeric, whereas b-crystallins exist as dimers to octamers in solution [7]. b-and c-crystallins are the prototype and founding members of the bc-crystallin superfamily [8,9]. Crystallins are the major proteins of a mammalian eye lens. The topologically similar eye lens proteins, b-and c-crystallins, are the prototype and founding members of the bc-crystallin superfamily. bc-Crystallins have until recently been regarded as structural proteins. However, the calciumbinding properties of a few members and the potential role of bc-crystallins in fertility are being investigated. Because the calcium-binding elements of other member proteins, such as spherulin 3a, are not present in bB2-crystallin and other bc-crystallins from fish and mammalian genomes, it was argued that lens bc-crystallins should not bind calcium. In order to probe whether b-crystallins can bind calcium, we selected one basic (bB2) and one acidic (bA3) b-crystallin for calcium-binding studies. Using calciumbinding assays such as 45 Ca overlay, terbium binding, Stains-All and isothermal titration calorimetry, we established that both bB2-and bA3-crystallin bind calcium with moderate affinity. There was no significant change in their conformation upon binding calcium as monitored by fluorescence and circular dichroism spectroscopy. However, 15 N-1 H heteronuclear single quantum correlation NMR spectroscopy revealed that amide environment of several residues underwent changes indicating calcium ligation. With the corroboration of calcium-binding to bB2-and bA3-crystallins, we suggest that all b-crystallins bind calcium. Our results have important implications for understanding the calcium-related cataractogenesis and maintenance of ionic homeostasis in the lens.Abbreviations AIM1, protein absent in melanoma 1; HSQC, heteronuclear single quantum correlation; ITC, isothermal titration calorimetry; PDB, protein databank; TCEP, Tris(2-carboxyethyl) phosphine hydrochloride.

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“…Several optical properties make the Ln(II1)'s useful and convenient: their redshifted visible emission, their long luminescent lifetimes, the sensitivity of their absorption and emission to environment, the overlap of their excited state manifolds with the excited states of biological ligands and finally, the variety of their emission properties which make intra-Ln(II1) transfer and luminescence quenching possible. The long history of Ln(II1) substitution into biochemical environments and spectroscopic analysis of the product is best summarized in the review by Horrocks (1982). By far, the greatest amount of biological information has been obtained from Ln(II1) substitutions into Ca(I1) binding sites in proteins.…”

Section: Introductionmentioning

confidence: 99%

Lanthanide Ions as Luminescent Probes of Biomolecular Structure

O’Hara¹

1987

Photochem & Photobiology

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Lanthanide ion luminescence probes of biomolecular structure

Cited by 6 publications

References 0 publications

The Chemistry of Lanthanides in Biology: Recent Discoveries, Emerging Principles, and Technological Applications

The Chemistry of Lanthanides in Biology: Recent Discoveries, Emerging Principles, and Technological Applications

Calcium‐binding to lens βB2‐ and βA3‐crystallins suggests that all β‐crystallins are calcium‐binding proteins

Lanthanide Ions as Luminescent Probes of Biomolecular Structure

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