Intrinsic (Gas-Phase) Binding of Co2+ and Ni2+ by Peptides: A Direct Reflection of Aqueous-Phase Chemistry

Reiter, Alex; Adams, Jeanette; Zhao, Hong Yan

doi:10.1021/ja00096a045

J. Am. Chem. Soc.

1994

DOI: 10.1021/ja00096a045

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Intrinsic (Gas-Phase) Binding of Co2+ and Ni2+ by Peptides: A Direct Reflection of Aqueous-Phase Chemistry

Alex Reiter¹,

Jeanette Adams²,

Hong Yan Zhao³

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Cited by 70 publications

(55 citation statements)

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“…A similar H 2 loss was also previously reported in CAD studies for Ni(II) bound dipeptides, where authors suggested the existence of isomers with two hydrides, H − , coordinating Ni(II) cation. 29 These findings confirm that hydrogen species such as H + and H − are rather free to migrate within a metal ion-bound complex, even across the metal ion, as shown in the formation of protonbound lysine monomer, (Nε-Acetyl-Lys+H) + , upon SORI-CAD application to Nε-Acetyl-L-Lys Zn(II) complexes, consistent with Wysockis mobile proton model. Proposed structures of bis-lysated zinc complex, (Zn+ Lys+Lys−H) + .…”

supporting

confidence: 78%

Tandem Mass Spectrometric Evidence for the Involvement of a Lysine Basic Side Chain in the Coordination of Zn(II) Ion within a Zinc-bound Lysine Ternary Complex

2004

Bulletin of the Korean Chemical Society

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We present the tandem mass spectrometry applications carried out to elucidate the coordination structure of Zn(II) bound lysine ternary complexes, (Zn+Lys+Lys−H) + , which is a good model system to represent a simple (metallo)enzyme-substrate complex (ES). In particular, experimental efforts were focused on revealing the involvement of a lysine side chain ε-amino group in the coordination of Zn 2+ divalent ions. MS/MS fragmentation pattern showed that all the oxygen species within a complex fell off in the form of H 2 O in contrast to those of other ternary complexes containing amino acids with simple side chains (4-coordinate geometries, Figure 1a), suggesting that the lysine complexes have different coordination structures from the others. The participation of a lysine basic side chain in the coordination of Zn(II) was experimentally evidenced in MS/MS for Nε-Acetyl-L-Lys Zn(II) complexes with acetyl protection groups as well as in MS/MS for the ternary complexes with one NH 3 loss, (Zn+Lys+Lys−NH 3 −H) + . Detailed structures were predicted using ab initio calculations on (Zn+Lys+Lys−H) + isomers with 4-, 5-, and 6-coordinate structures. A zwitterionic 4-coordinate complex ( Figure 7d) and a 5-coordinate structure with distorted bipyramidal geometry (Figure 7b) are found to be most plausible in terms of energy stability and compatibility with the experimental observations, respectively.

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supporting

confidence: 78%

Tandem Mass Spectrometric Evidence for the Involvement of a Lysine Basic Side Chain in the Coordination of Zn(II) Ion within a Zinc-bound Lysine Ternary Complex

2004

Bulletin of the Korean Chemical Society

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“…With the development of gentle ionization techniques such as ESI [29,30] and MALDI [31,32] for transferring peptides/proteins into the gas phase without detrimental effects on their integrity, mass spectrometry has been used successfully to characterize metal cation (such as calcium, cadmium, cobalt, copper, iron, magnesium, mercury, nickel, potassium, sodium, and zinc) peptide/protein interactions [33][34][35][36][37][38][39][40][41][42][43][44][45][46]. Data reveals some general findings such as various metal ions may interact differently to a peptide sequence [33,47], and the metal cation-peptide/protein bond is believed to be noncovalent [33].…”

mentioning

confidence: 99%

Gold Ion–Angiotensin Peptide Interaction by Mass Spectrometry

Lee

Jayathilaka

Gupta

et al. 2012

J. Am. Soc. Mass Spectrom.

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Stimulated by the interest in developing gold compounds for treating cancer, gold ionangiotensin peptide interactions are investigated by mass spectrometry. Under the experimental conditions used, the majority of gold ion-angiotensin peptide complexes contain gold in the oxidation states I and III. Both ESI-MS and MALDI-TOF MS detect singly/multiply charged ions for mononuclear/multinuclear gold-attached peptides, which are represented as [peptide+a Au (I)+b Au(III)+(e -a -3b) H] e+ , where a,b≥0 and e is charge. ESI-MS data shows singly/multiply charged ions of Au(I)-peptide and Au(III)-peptide complexes. This study reveals that MALDI-TOF MS mainly detects singly charged Au(I)-peptide complexes, presumably due to the ionization process. The electrons in the MALDI plume seem to efficiently reduce Au(III) to Au(I). MALDI also tends to enhance the higher polymeric forms of gold-peptide complexes regardless of the laser power used. Collision-induced dissociation experiments of the mononuclear and dinuclear gold-attached peptide ions for angiotensin peptides show that the gold ion (a soft acid) binding sites are in the vicinity of Cys (a soft ligand), His (a major anchor of peptide for metal ion chelation), and the basic residue Arg. Data also suggests that the abundance of gold-attached peptides increases with higher gold concentration until saturation, after which an increase in gold ion concentration leads to the aggregation and/or precipitation of gold-bound peptides.

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“…Intrinsic interactions of divalent metal ions with amino acids [10], peptides [11][12][13][14][15][16][17][18][19][20][21][22], and proteins [17,18,[23][24][25] have been extensively characterized in the gas phase by different techniques, including collision activated dissociation (CAD), ion mobility mass spectrometry, and hydrogen/deuterium exchange. For example, Gross and coworkers performed CAD of Ca 2ϩ complexes with peptide analogs of the calcium binding-site III of rabbit skeletal troponin C and found that Ca 2ϩ is bound to deprotonated acidic sites and carbonyl oxygens [14].…”

mentioning

confidence: 99%

Divalent metal ion-peptide interactions probed by electron capture dissociation of trications

Liu

Håkansson

2006

J. Am. Soc. Mass Spectrom.

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Electron capture dissociation (ECD) of the peptide Substance P (SubP) complexed with divalent metals has been investigated. ECD of [SubP ϩ H ϩ M] 3ϩ (M 2ϩ ϭ Mg 2ϩ -Ba 2ϩ and Mn 2ϩ -Zn 2ϩ ) allowed observation of a larger number of product ions than previous investigations of doubly charged metal-containing peptides. ECD of Mg-Ba, Mn, Fe, and Zn-containing complexes resulted in product ions with and without the metal from cleavage of backbone amine bonds (c= and z · -type ions). By contrast, ECD of Co and Ni-containing complexes yielded major bond cleavages within the C-terminal methionine residue (likely to be the metal ion binding site). Cu-containing complexes displayed yet another behavior: amide bond cleavage (b and y=-type ions). We believe some results can be rationalized both within the hot hydrogen atom mechanism and mechanisms involving electron capture into excited states, such as the recently proposed amide superbase mechanism. However, some behavior, including formation of (c n =M Ϫ H) ϩ ions for Ca-Ba, is best explained within the latter mechanisms with initial electron capture at the metal. In addition, the ECD behavior appears to correlate with the metal second ionization energy (IE2). Co and Ni (displaying sequestered fragmentation) have IE2s of 17.1 and 18.2 eV, respectively, whereas IE2s for Mg-Ba, Mn, and Fe (yielding random cleavage) are 10.0 to 16.2 eV. This behavior is difficult to explain within the hot hydrogen atom mechanism because hydrogen transfer should not be influenced by IE2s. However, the drastically different fragmentation patterns for Co, Ni, and Cu compared to the other metals can also be explained by their higher propensity for nitrogen (as opposed to oxygen) binding. Nevertheless, these results imply that directed fragmentation can be accomplished via careful

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Intrinsic (Gas-Phase) Binding of Co2+ and Ni2+ by Peptides: A Direct Reflection of Aqueous-Phase Chemistry

Cited by 70 publications

References 0 publications

Tandem Mass Spectrometric Evidence for the Involvement of a Lysine Basic Side Chain in the Coordination of Zn(II) Ion within a Zinc-bound Lysine Ternary Complex

Tandem Mass Spectrometric Evidence for the Involvement of a Lysine Basic Side Chain in the Coordination of Zn(II) Ion within a Zinc-bound Lysine Ternary Complex

Gold Ion–Angiotensin Peptide Interaction by Mass Spectrometry

Divalent metal ion-peptide interactions probed by electron capture dissociation of trications

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