ArticleProtein science : a publication of the Protein Society2002
Probing metal ion binding and conformational properties of the colicin E9 endonuclease by electrospray ionization time-of-flight mass spectrometry.
Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed, 60 citations in OpenAlex.
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- Stabilization of protein structure through π-π interaction in the second coordination sphere of pseudoazurin.Protein science : a publication of the Protein Society · 2017Article
- The conformational response to Zn(II) and Ni(II) binding of Sporosarcina pasteurii UreG, an intrinsically disordered GTPase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
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- Fine tuning of the catalytic activity of colicin E7 nuclease domain by systematic N-terminal mutations.Protein science : a publication of the Protein Society · 2014Article
- Mass spectrometry-based methods to study protein architecture and dynamics.Protein science : a publication of the Protein Society · 2013Review
- The role of the N-terminal loop in the function of the colicin E7 nuclease domain.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
- Transferrin as a model system for method development to study structure, dynamics and interactions of metalloproteins using mass spectrometry.Biochimica et biophysica acta · 2012Review
- Electrospray ionization mass spectrometry: a technique to access the information beyond the molecular weight of the analyte.International journal of analytical chemistry · 2012Article
- Advanced mass spectrometry-based methods for the analysis of conformational integrity of biopharmaceutical products.Current pharmaceutical biotechnology · 2011Review
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- Zinc ion-induced domain organization in metallo-beta-lactamases: a flexible "zinc arm" for rapid metal ion transfer?The Journal of biological chemistry · 2009Article
- Widespread distribution of cell defense against D-aminoacyl-tRNAs.The Journal of biological chemistry · 2009Article
- Analysis of protein-protein interaction surfaces using a combination of efficient lysine acetylation and nanoLC-MALDI-MS/MS applied to the E9:Im9 bacteriotoxin--immunity protein complex.Journal of the American Society for Mass Spectrometry · 2006Article
- Crystal structural analysis and metal-dependent stability and activity studies of the ColE7 endonuclease domain in complex with DNA/Zn2+ or inhibitor/Ni2+.Protein science : a publication of the Protein Society · 2006Article
- Monitoring the zinc affinity of the metallo-beta-lactamase CphA by automated nanoESI-MS.Journal of the American Society for Mass Spectrometry · 2006Article
- Multidimensional separations of ubiquitin conformers in the gas phase: relating ion cross sections to H/D exchange measurements.Journal of the American Society for Mass Spectrometry · 2005Article
- Binding of a diphosphorylated-ITAM peptide to spleen tyrosine kinase (Syk) induces distal conformational changes: a hydrogen exchange mass spectrometry study.Journal of the American Society for Mass Spectrometry · 2005Article
- Real-time monitoring of enzymatic DNA hydrolysis by electrospray ionization mass spectrometry.Nucleic acids research · 2005Article
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7 authors at 3 institutions in 2 countries.
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Abstract
Nano-electrospray ionization time-of-flight mass spectrometry (ESI-MS) was used to study the conformational consequences of metal ion binding to the colicin E9 endonuclease (E9 DNase) by taking advantage of the unique capability of ESI-MS to allow simultaneous assessment of conformational heterogeneity and metal ion binding. Alterations of charge state distributions on metal ion binding/release were correlated with spectral changes observed in far- and near-UV circular dichroism (CD) and intrinsic tryptophan fluorescence. In addition, hydrogen/deuterium (H/D) exchange experiments were used to probe structural integrity. The present study shows that ESI-MS is sensitive to changes of the thermodynamic stability of E9 DNase as a result of metal ion binding/release in a manner consistent with that deduced from proteolysis and calorimetric experiments. Interestingly, acid-induced release of the metal ion from the E9 DNase causes dramatic conformational instability associated with a loss of fixed tertiary structure, but secondary structure is retained. Furthermore, ESI-MS enabled the direct observation of the noncovalent protein complex of E9 DNase bound to its cognate immunity protein Im9 in the presence and absence of Zn(2+). Gas-phase dissociation experiments of the deuterium-labeled binary and ternary complexes revealed that metal ion binding, not Im9, results in a dramatic exchange protection of E9 DNase in the complex. In addition, our metal ion binding studies and gas-phase dissociation experiments of the ternary E9 DNase-Zn(2+)-Im9 complex have provided further evidence that electrostatic interactions govern the gas phase ion stability.
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