Advanced nuclear analytical techniques for metalloproteomics

Gao, Yuxi; Chen, Chunying; Chai, Zhifang

doi:10.1039/b703323k

Cited by 58 publications

(43 citation statements)

References 121 publications

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“…The X-ray absorption spectrum is presented as a function of the X-ray energy and can be divided into two regions, the near edge (XANES) and beyond the edge (EXAFS). XANES gives information about oxidation state, covalence, and molecular symmetry of the site as well as the coordination number; whereas EXAFS provides structural information about the metal-binding environment, such as the coordination number, the identity of the ligands (coordination atoms e.g., O, N or S), and the distance between the metal and each ligand [32] . XAS can be conveniently used to examine structurefunction relationships, such as the spatial distribution, chemical speciation of elements and the oxidation states of metals and metalloids in a wide range of environmental and biological samples.…”

Section: Structure-function Studies Of Metalloproteinsmentioning

confidence: 99%

“…The traditional tools of structural determination are X-ray crystallography [91] and nuclear magnetic resonance (NMR) [92] . In addition, some other techniques, such as Mössbauer spectroscopy, X-ray absorption spectrometry (XAS), electron paramagnetic resonance (EPR), resonance Raman spectroscopy (RR) and magnetic circular dichroism (MCD) are needed for the detailed structural characterizations of the metal sites in metalloproteins [32,[93][94][95] . Here we will focus only on the application of XAS in structure-function studies of metalloproteins.…”

Section: Structure-function Studies Of Metalloproteinsmentioning

confidence: 99%

“…This review will focus only on the identification of seleno-/phospho-/metallo-proteins, structure-function relationships of metalloproteins and clinically used metallodrugs, as well as the discussion of the relevant analytical approaches. Readers are referred to some other excellent reviews in this field, either general (e.g., Haraguchi [22] , Łobinśki et al [21,27] , Sun et al [28] , Chance et al [23] , Szpunar [20] , Bettmer [25] , López-Barea and Gómez-Ariza [29] ) or method-oriented (e.g., Łobinśki et al [10,17] , Shah and Caruso [18] , Aebersold and Mann [16] , Szpunar [30] , Chance et al [31] , Gao et al [32] , Prange and Pröfrock [33] ).…”

Section: Introductionmentioning

confidence: 97%

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Metallomics: An integrated biometal science

Sun

2009

Sci. China Ser. B-Chem.

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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

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Section: Structure-function Studies Of Metalloproteinsmentioning

confidence: 99%

Section: Structure-function Studies Of Metalloproteinsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 97%

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Metallomics: An integrated biometal science

Sun

2009

Sci. China Ser. B-Chem.

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“…These atomic detectors include nuclear techniques such as autoradiography and neutron activation analysis (NAA); X-ray techniques such as particle induced X-ray emission (PIXE), X-ray absorption spectroscopy (XAS) and X-ray fluorescence (XRF); or atomic absorption techniques such as flame atomic absorption spectrometry (FAAS) and electrothermal atomic absorption spectrometry (ETAAS) [78][79]. However, the use of inductively coupled plasma mass spectrometry (ICP-MS) has been relegated to the background of these conventional nuclear techniques in metallomic investigations.…”

Section: Separation Techniquesmentioning

confidence: 99%

Size Fractionation of Metal Species from Serum Samples for Studying Element Biodistribution in Alzheimer’s Disease

González‐Domínguez

2017

Neuromethods

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This work considers the development of a novel analytical procedure for rapid and simple size fractionation of metal species from human serum samples, with a great potential for studying characteristic abnormalities of metal homeostasis associated with Alzheimer's disease and other neurodegenerative disorders. For this purpose, serum samples are subjected to protein precipitation under non-denaturing conditions, taking special care for maintaining the integrity of metal-biomolecule bindings and for preventing species transformation, and then both the supernatant (low molecular mass fraction) and the precipitate (high molecular mass fraction) are analyzed by ICP-MS in order to determine the biodistribution of serum trace elements. This methodology is validated for 11 trace elements, including aluminum, cadmium, cobalt, chromium, copper, iron, manganese, molybdenum, selenium, vanadium, and zinc, in terms of sensitivity, selectivity, accuracy, and precision.

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“…Because metals constitute about one third of proteins, and are crucial to maintain the functions and structures of the proteins (Gao, Chen, & Chai, 2007), the identification and quantification of metal-containing proteins is another great challenge in proteomics study. Although the molecular mass spectrometry has played an important role in proteomics, it alone seems to be unable to solve problems that are relevant to metal-containing proteins because of their insufficient detection limits of metals in real-world salt-rich matrices (Lobinski, Schaumlöffel, & Szpunar, 2006).…”

mentioning

confidence: 99%

ICP‐MS‐Based strategies for protein quantification

Wang

Feng

Zhao

et al. 2009

Mass Spectrometry Reviews

108

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In the post-genomics era, proteomics has become a central branch in life sciences. An understanding of biological functions will not only rely on protein identification, but also on protein quantification in a living organism. Most of the existing methods for quantitative proteomics are based on isotope labeling combined with molecular mass spectrometry. Recently, a remarkable progress that utilizes inductively coupled plasma-mass spectrometry (ICP-MS) as an attractive complement to electrospray MS and MALDI MS for protein quantification, especially for absolute quantification, has been achieved. This review will selectively discuss the recent advances of ICP-MS-based technique, which will be expected to further mature and to become one of the key methods in quantitative proteomics.

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Advanced nuclear analytical techniques for metalloproteomics

Cited by 58 publications

References 121 publications

Metallomics: An integrated biometal science

Metallomics: An integrated biometal science

Size Fractionation of Metal Species from Serum Samples for Studying Element Biodistribution in Alzheimer’s Disease

ICP‐MS‐Based strategies for protein quantification

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