Metallomics: An integrated biometal science

Abstract

Metallomics is an emerging scientific area integrating the research fields related to the understanding of the molecular mechanisms of metal-associated life processes and the entirety of metal and metalloid species within a cell or tissue type. In metallomics, metalloproteins, metalloenzymes and other metalcontaining biomolecules in a biological system are referred to as metallomes, similar to genomes and proteomes in genomics and proteomics, respectively. This review discusses the concept of metallomics with a focus on analytical techniques and methods, particularly the so-called hyphenated techniques which combine a high-resolution separation technique (gel electrophoresis/laser ablation, chromatography or capillary electrophoresis) with a highly sensitive detection method such as elemental (inductively coupled plasma, ICP) or molecular (electron spray ionization (ESI) or matrix-assisted laser desorption/ionization (MALDI)) mass spectrometry, or nuclear X-ray fluorescence/ absorption spectrometry. The applications of these advanced analytical methods in the identification of metallo-/phospho-/seleno-proteins, probing of relationships between structure and function of metalloproteins, and study of clinically used metallodrugs will be selectively outlined, along with their advantages and limitations. metallomics, metallome, metallodrug, metalloprotein, chemical speciation

Bacterial Phosphoproteomic Analysis Reveals the Correlation Between Protein Phosphorylation and Bacterial Pathogenicity

“…However, due to the very low stoichiometry, limited dynamic range, high complexity and quantitative difficulties of protein phosphorylations, highly selective enrichment procedures and sensitive mass spectrometry (MS) are required to decipher the phosphoproteome ( 4 ) . Selective phosphopeptide enrichment has been accomplished in several ways by using anti-phosphotyrosine antibodies, immobilized metal affinity chromatography (IMAC), chemical modifications or strong cation exchange chromatography ( 5 ) . The seamless combination of IMAC and nano-liquid chromatography enables reproducible separation and identification of phosphopeptides in a low-femtomole range 6 , 7 , and thus it is the most frequently used method in the study of cellular phosphorylation.…”

Phosphoproteome analysis of the pathogenic bacterium Helicobacter pylori reveals over‐representation of tyrosine phosphorylation and multiply phosphorylated proteins

“…However, due to the very low stoichiometry, limited dynamic range, high complexity and quantitative difficulties of protein phosphorylations, highly selective enrichment procedures and sensitive MS are required to decipher the phosphoproteome 3. Selective phosphopeptide enrichment has been accomplished in several ways by using antiphosphotyrosine antibodies, immobilized metal affinity chromatography (IMAC), chemical modifications or strong cation exchange chromatography 4. The seamless combination of IMAC and nano‐LC enables reproducible separation and identification of phosphopeptides in a low‐femtomole range 5, 6, and thus it is the most frequently used method in the study of cellular phosphorylation.…”

Precise, fast and flexible determination of protein interactions by affinity capillary electrophoresis. Part 2: Cations

“…The binding of metal ions to proteins is of particular interest [3,[19][20][21]. Meanwhile an own research topic metallomics has even been established [20,21]. Usually metal ions interact with protein-binding sites containing histidine, cysteine, glutamic acid, aspartic acid, lysine, phosphate, and others [19,22].…”

“…The binding of metal ions to proteins is of particular interest . Meanwhile an own research topic metallomics has even been established .…”