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Journal articles on the topic 'Metal-binding proteins'

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Published: 10 March 2023

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1

Permyakov, Eugene A. "Metal Binding Proteins." Encyclopedia 1, no. 1 (March 15, 2021): 261–92. http://dx.doi.org/10.3390/encyclopedia1010024.

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Metal ions play several major roles in proteins: structural, regulatory, and enzymatic. The binding of some metal ions increase stability of proteins or protein domains. Some metal ions can regulate various cell processes being first, second, or third messengers. Some metal ions, especially transition metal ions, take part in catalysis in many enzymes. From ten to twelve metals are vitally important for activity of living organisms: sodium, potassium, magnesium, calcium, manganese, iron, cobalt, zinc, nickel, vanadium, molybdenum, and tungsten. This short review is devoted to structural, physical, chemical, and physiological properties of proteins, which specifically bind these metal cations.

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2

Hennig, H. F. K. O. "Metal-Binding Proteins as Metal Pollution Indicators." Environmental Health Perspectives 65 (March 1986): 175. http://dx.doi.org/10.2307/3430178.

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3

Hennig, H. F. "Metal-binding proteins as metal pollution indicators." Environmental Health Perspectives 65 (March 1986): 175–87. http://dx.doi.org/10.1289/ehp.8665175.

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4

Findlay, Wendy A., Gary S. Shaw, and Brian D. Sykes. "Metal-ion binding by proteins." Current Biology 2, no. 3 (March 1992): 126. http://dx.doi.org/10.1016/0960-9822(92)90246-7.

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5

Tainer, John A., Victoria A. Roberts, and Elizabeth D. Getzoff. "Metal-binding sites in proteins." Current Opinion in Biotechnology 2, no. 4 (August 1991): 582–91. http://dx.doi.org/10.1016/0958-1669(91)90084-i.

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6

Findlay, Wendy A., Gary S. Shaw, and Brian D. Sykes. "Metal ion binding by proteins." Current Opinion in Structural Biology 2, no. 1 (February 1992): 57–60. http://dx.doi.org/10.1016/0959-440x(92)90177-9.

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7

Berg, Jeremy M. "Nucleic acid-binding proteins: More metal-binding fingers." Nature 319, no. 6051 (January 1986): 264–65. http://dx.doi.org/10.1038/319264a0.

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8

MOHAN, ABHILASH, SHARMILA ANISHETTY, and PENNATHUR GAUTAM. "GLOBAL METAL-ION BINDING PROTEIN FINGERPRINT: A METHOD TO IDENTIFY MOTIF-LESS METAL-ION BINDING PROTEINS." Journal of Bioinformatics and Computational Biology 08, no. 04 (August 2010): 717–26. http://dx.doi.org/10.1142/s0219720010004884.

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Metal-ion binding proteins play a vital role in biological processes. Identifying putative metal-ion binding proteins is through knowledge-based methods. These involve the identification of specific motifs that characterize a specific class of metal-ion binding protein. Metal-ion binding motifs have been identified for the common metal ions. A robust global fingerprint that is useful in identifying a metal-ion binding protein from a non-metal-ion binding protein has not been devised. Such a method will help in identifying novel metal-ion binding proteins and proteins that do not possess a canonical metal-ion binding motif. We have used a set of physico-chemical parameters of metal-ion binding proteins encoded by the genes CzcA, CzcB and CzcD as a training set to supervised classifiers and have been able to identify several other metal ion binding proteins leading us to believe that metal-ion binding proteins have a global fingerprint, which cannot be pinned down to a single feature of the protein sequence.

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9

Lu, Yi, and Joan S. Valentine. "Engineering metal-binding sites in proteins." Current Opinion in Structural Biology 7, no. 4 (August 1997): 495–500. http://dx.doi.org/10.1016/s0959-440x(97)80112-1.

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10

Klemba, Michael, Kevin H. Gardner, Stephen Marino, Neil D. Clarke, and Lynne Regan. "Novel metal-binding proteins by design." Nature Structural & Molecular Biology 2, no. 5 (May 1995): 368–73. http://dx.doi.org/10.1038/nsb0595-368.

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11

Berg, J. "Potential metal-binding domains in nucleic acid binding proteins." Science 232, no. 4749 (April 25, 1986): 485–87. http://dx.doi.org/10.1126/science.2421409.

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12

Konovalov, Yu D. "Metal-binding Proteins of Mature Fish Eggs." Hydrobiological Journal 37, no. 4 (2001): 13. http://dx.doi.org/10.1615/hydrobj.v37.i4.110.

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13

Davies, Paul, Sarah N. Fontaine, Dima Moualla, Xiaoyan Wang, Josephine A. Wright, and David R. Brown. "Amyloidogenic metal-binding proteins: new investigative pathways." Biochemical Society Transactions 36, no. 6 (November 19, 2008): 1299–303. http://dx.doi.org/10.1042/bst0361299.

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Neurodegenerative diseases remain perplexing and problematic for modern research. Those associated with amyloidogenic proteins have often been lumped together simply because those proteins aggregate. However, research has identified a more logical reason to group some of these diseases together. The associated proteins not only aggregate, but also bind copper. The APP (amyloid precursor protein) binds copper in an N-terminal region. Binding of copper has been suggested to influence generation of β-amyloid from the protein. PrP (prion protein) binds copper, and this appears to be necessary for its normal function and might also reduce its probability of conversion into an infectious prion. α-Synuclein, a protein associated with Parkinson's disease, also binds copper, but, in this case, it potentially increases the rate at which the protein aggregates. The similarities between these proteins, in terms of metal binding, has allowed us to investigate them using similar approaches. In the present review, we discuss some of these approaches.

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14

Miller, Matthew B., Alexis M. Clough, Jennifer N. Batson, and Richard W. Vachet. "Transition metal binding to cod otolith proteins." Journal of Experimental Marine Biology and Ecology 329, no. 1 (February 2006): 135–43. http://dx.doi.org/10.1016/j.jembe.2005.08.016.

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15

Dudev, Todor, and Carmay Lim. "Metal Binding and Selectivity in Zinc Proteins." Journal of the Chinese Chemical Society 50, no. 5 (October 2003): 1093–102. http://dx.doi.org/10.1002/jccs.200300155.

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16

Arnold, F., and B. Haymore. "Engineered metal-binding proteins: purification to protein folding." Science 252, no. 5014 (June 28, 1991): 1796–97. http://dx.doi.org/10.1126/science.1648261.

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17

Regan, L. "The Design of Metal-Binding Sites in Proteins." Annual Review of Biophysics and Biomolecular Structure 22, no. 1 (June 1993): 257–81. http://dx.doi.org/10.1146/annurev.bb.22.060193.001353.

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18

Song, Lin Frank, Arkajyoti Sengupta, and Kenneth M. Merz. "Thermodynamics of Transition Metal Ion Binding to Proteins." Journal of the American Chemical Society 142, no. 13 (March 6, 2020): 6365–74. http://dx.doi.org/10.1021/jacs.0c01329.

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19

Qu, Jing, Sheng S. Yin, and Han Wang. "Prediction of Metal Ion Binding Sites of Transmembrane Proteins." Computational and Mathematical Methods in Medicine 2021 (October 22, 2021): 1–11. http://dx.doi.org/10.1155/2021/2327832.

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The metal ion binding of transmembrane proteins (TMPs) plays a fundamental role in biological processes, pharmaceutics, and medicine, but it is hard to extract enough TMP structures in experimental techniques to discover their binding mechanism comprehensively. To predict the metal ion binding sites for TMPs on a large scale, we present a simple and effective two-stage prediction method TMP-MIBS, to identify the corresponding binding residues using TMP sequences. At present, there is no specific research on the metal ion binding prediction of TMPs. Thereby, we compared our model with the published tools which do not distinguish TMPs from water-soluble proteins. The results in the independent verification dataset show that TMP-MIBS has superior performance. This paper explores the interaction mechanism between TMPs and metal ions, which is helpful to understand the structure and function of TMPs and is of great significance to further construct transport mechanisms and identify potential drug targets.

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20

Gregory, David S., Andrew C. R. Martin, Janet C. Cheetham, and Anthony R. Rees. "The prediction and characterization of metal binding sites in proteins." "Protein Engineering, Design and Selection" 6, no. 1 (1993): 29–35. http://dx.doi.org/10.1093/protein/6.1.29.

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21

Samuelson, Patrik, Henrik Wernérus, Malin Svedberg, and Stefan Ståhl. "Staphylococcal Surface Display of Metal-Binding Polyhistidyl Peptides." Applied and Environmental Microbiology 66, no. 3 (March 1, 2000): 1243–48. http://dx.doi.org/10.1128/aem.66.3.1243-1248.2000.

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ABSTRACT Recombinant Staphylococcus xylosus andStaphylococcus carnosus strains were generated with surface-exposed chimeric proteins containing polyhistidyl peptides designed for binding to divalent metal ions. Surface accessibility of the chimeric surface proteins was demonstrated and the chimeric surface proteins were found to be functional in terms of metal binding, since the recombinant staphylococcal cells were shown to have gained Ni2+- and Cd2+-binding capacity, suggesting that such bacteria could find use in bioremediation of heavy metals. This is, to our knowledge, the first time that recombinant, surface-exposed metal-binding peptides have been expressed on gram-positive bacteria. Potential environmental or biosensor applications for such recombinant staphylococci as biosorbents are discussed.

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22

Shoeib, Tamer, and Zoltán Mester. "Towards the characterization of metal binding proteins in metal enriched yeast." Microchemical Journal 85, no. 2 (April 2007): 329–40. http://dx.doi.org/10.1016/j.microc.2006.08.001.

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23

Vogel, Manja, Sabine Matys, Falk Lehmann, Björn Drobot, Tobias Günther, Katrin Pollmann, and Johannes Raff. "Use of Specific Metal Binding of Self-Assembling S-Layer Proteins for Metal Bioremediation and Recycling." Solid State Phenomena 262 (August 2017): 389–93. http://dx.doi.org/10.4028/www.scientific.net/ssp.262.389.

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Most bacteria and all archaea possess as outermost cell envelope so called surface-layers (S-layers). These layers were formed by self-assembling proteins having a number of habitat depending interesting intrinsic properties. As example, S-layers from bacterial isolates recovered from heavy metal contaminated environments have outstanding metal binding properties and are highly stable. Thus they selectively bind several metals with different affinity. For using S-layer proteins for metal bioremediation and recycling three aspects of the metal-interactions with S-layer proteins must be taken into account. First, S-layers possess different functionalities, e.g. carboxyl, phosphoryl groups, binding toxic metals and metalloids, like U(VI) and As(V), nonspecifically depending on pH. Second, precious metals like Au and Pd are likewise nonspecifically bound to functional groups, but presumably covalently, making the binding irreversible. Third, intrinsic specifically bound metals, e.g. Ca2+, are needed for native protein folding, self-assembly, and the formation of highly-ordered lattices. Their binding sites also allow selective binding of chemical-equal elements including the trivalent rare earth elements, possessing comparable ionic radii. Thus this study combines older and recently generated results regarding the metal dependent binding behavior of the S-layer proteins. It enables the development of biohybrid materials for the separation, removal or recovery of strategic relevant metals from natural occurring or industrial waste waters using pH-value as regulating parameter for selective metal binding and also conceivably release.

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24

Wernérus, Henrik, Janne Lehtiö, Tuula Teeri, Per-Åke Nygren, and Stefan Ståhl. "Generation of Metal-Binding Staphylococci through Surface Display of Combinatorially Engineered Cellulose-Binding Domains." Applied and Environmental Microbiology 67, no. 10 (October 1, 2001): 4678–84. http://dx.doi.org/10.1128/aem.67.10.4678-4684.2001.

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ABSTRACT Ni2+-binding staphylococci were generated through surface display of combinatorially engineered variants of a fungal cellulose-binding domain (CBD) from Trichoderma reeseicellulase Cel7A. Novel CBD variants were generated by combinatorial protein engineering through the randomization of 11 amino acid positions, and eight potentially Ni2+-binding CBDs were selected by phage display technology. These new variants were subsequently genetically introduced into chimeric surface proteins for surface display on Staphylococcus carnosus cells. The expressed chimeric proteins were shown to be properly targeted to the cell wall of S. carnosus cells, since full-length proteins could be extracted and affinity purified. Surface accessibility for the chimeric proteins was demonstrated, and furthermore, the engineered CBDs, now devoid of cellulose-binding capacity, were shown to be functional with regard to metal binding, since the recombinant staphylococci had gained Ni2+-binding capacity. Potential environmental applications for such tailor-made metal-binding bacteria as bioadsorbents in biofilters or biosensors are discussed.

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25

Jia, Shuailong, Runjing Wang, Kui Wu, Hongliang Jiang, and Zhifeng Du. "Elucidation of the Mechanism of Action for Metal Based Anticancer Drugs by Mass Spectrometry-Based Quantitative Proteomics." Molecules 24, no. 3 (February 6, 2019): 581. http://dx.doi.org/10.3390/molecules24030581.

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The discovery of the anticancer activity of cisplatin and its clinical application has opened a new field for studying metal-coordinated anticancer drugs. Metal-based anticancer drugs, such as cisplatin, can be transported to cells after entering into the human body and form metal–DNA or metal–protein adducts. Then, responding proteins will recognize adducts and form stable complexes. The proteins that were binding with metal-based anticancer drugs were relevant to their mechanism of action. Herein, investigation of the recognition between metal-based anticancer drugs and its binding partners will further our understanding about the pharmacology of cytotoxic anticancer drugs and help optimize the structure of anticancer drugs. The “soft” ionization mass spectrometric methods have many advantages such as high sensitivity and low sample consumption, which are suitable for the analyses of complex biological samples. Thus, MS has become a powerful tool for the identification of proteins binding or responding to metal-based anticancer drugs. In this review, we focused on the mass spectrometry-based quantitative strategy for the identification of proteins specifically responding or binding to metal-based anticancer drugs, ultimately elucidating their mechanism of action.

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26

Garg, Aditi, and Debnath Pal. "Inferring metal binding sites in flexible regions of proteins." Proteins: Structure, Function, and Bioinformatics 89, no. 9 (April 26, 2021): 1125–33. http://dx.doi.org/10.1002/prot.26085.

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27

McLeary, Fleur, Alexandre Rcom-H’cheo-Gauthier, Michael Goulding, Rowan Radford, Yuho Okita, Peter Faller, Roger Chung, and Dean Pountney. "Switching on Endogenous Metal Binding Proteins in Parkinson’s Disease." Cells 8, no. 2 (February 19, 2019): 179. http://dx.doi.org/10.3390/cells8020179.

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The formation of cytotoxic intracellular protein aggregates is a pathological signature of multiple neurodegenerative diseases. The principle aggregating protein in Parkinson’s disease (PD) and atypical Parkinson’s diseases is α-synuclein (α-syn), which occurs in neural cytoplasmic inclusions. Several factors have been found to trigger α-syn aggregation, including raised calcium, iron, and copper. Transcriptional inducers have been explored to upregulate expression of endogenous metal-binding proteins as a potential neuroprotective strategy. The vitamin-D analogue, calcipotriol, induced increased expression of the neuronal vitamin D-dependent calcium-binding protein, calbindin-D28k, and this significantly decreased the occurrence of α-syn aggregates in cells with transiently raised intracellular free Ca, thereby increasing viability. More recently, the induction of endogenous expression of the Zn and Cu binding protein, metallothionein, by the glucocorticoid analogue, dexamethasone, gave a specific reduction in Cu-dependent α-syn aggregates. Fe accumulation has long been associated with PD. Intracellularly, Fe is regulated by interactions between the Fe storage protein ferritin and Fe transporters, such as poly(C)-binding protein 1. Analysis of the transcriptional regulation of Fe binding proteins may reveal potential inducers that could modulate Fe homoeostasis in disease. The current review highlights recent studies that suggest that transcriptional inducers may have potential as novel mechanism-based drugs against metal overload in PD.

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28

Vidossich, Pietro, and Alessandra Magistrato. "QM/MM Molecular Dynamics Studies of Metal Binding Proteins." Biomolecules 4, no. 3 (July 8, 2014): 616–45. http://dx.doi.org/10.3390/biom4030616.

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29

Kirberger, Michael, Hing C. Wong, Jie Jiang, and Jenny J. Yang. "Metal toxicity and opportunistic binding of Pb2+ in proteins." Journal of Inorganic Biochemistry 125 (August 2013): 40–49. http://dx.doi.org/10.1016/j.jinorgbio.2013.04.002.

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30

Jensen, M. Ringkjøbing, M. A. S. Hass, D. F. Hansen, and J. J. Led. "Investigating metal-binding in proteins by nuclear magnetic resonance." Cellular and Molecular Life Sciences 64, no. 9 (March 31, 2007): 1085–104. http://dx.doi.org/10.1007/s00018-007-6447-x.

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31

Choi, Yoojin, Sang Yup Lee, and Doh Chang Lee. "Biosynthesis of single nanoparticles using various metal binding proteins." New Biotechnology 31 (July 2014): S173. http://dx.doi.org/10.1016/j.nbt.2014.05.890.

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32

DeSilva, Tara M., Gianluigi Veglia, Fernando Porcelli, Andrew M. Prantner, and Stanley J. Opella. "Selectivity in heavy metal- binding to peptides and proteins." Biopolymers 64, no. 4 (June 3, 2002): 189–97. http://dx.doi.org/10.1002/bip.10149.

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33

Denesyuk, Alexander I., Sergei E. Permyakov, Mark S. Johnson, Eugene A. Permyakov, and Konstantin Denessiouk. "Building kit for metal cation binding sites in proteins." Biochemical and Biophysical Research Communications 494, no. 1-2 (December 2017): 311–17. http://dx.doi.org/10.1016/j.bbrc.2017.10.034.

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34

Sobolev, Vladimir, and Marvin Edelman. "Web Tools for Predicting Metal Binding Sites in Proteins." Israel Journal of Chemistry 53, no. 3-4 (April 2013): 166–72. http://dx.doi.org/10.1002/ijch.201200084.

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35

Furumura, Minao, Francisco Solano, Naoko Matsunaga, Chie Sakai, Richard A. Spritz, and Vincent J. Hearing. "Metal Ligand-Binding Specificities of the Tyrosinase-Related Proteins." Biochemical and Biophysical Research Communications 242, no. 3 (January 1998): 579–85. http://dx.doi.org/10.1006/bbrc.1997.8007.

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36

Sadakane, Yutaka, and Masahiro Kawahara. "Implications of Metal Binding and Asparagine Deamidation for Amyloid Formation." International Journal of Molecular Sciences 19, no. 8 (August 19, 2018): 2449. http://dx.doi.org/10.3390/ijms19082449.

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Increasing evidence suggests that amyloid formation, i.e., self-assembly of proteins and the resulting conformational changes, is linked with the pathogenesis of various neurodegenerative disorders such as Alzheimer’s disease, prion diseases, and Lewy body diseases. Among the factors that accelerate or inhibit oligomerization, we focus here on two non-genetic and common characteristics of many amyloidogenic proteins: metal binding and asparagine deamidation. Both reflect the aging process and occur in most amyloidogenic proteins. All of the amyloidogenic proteins, such as Alzheimer’s β-amyloid protein, prion protein, and α-synuclein, are metal-binding proteins and are involved in the regulation of metal homeostasis. It is widely accepted that these proteins are susceptible to non-enzymatic posttranslational modifications, and many asparagine residues of these proteins are deamidated. Moreover, these two factors can combine because asparagine residues can bind metals. We review the current understanding of these two common properties and their implications in the pathogenesis of these neurodegenerative diseases.

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37

Sauser, Luca, and Michal S. Shoshan. "Enhancing Metal-binding with Noncanonical Coordinating Amino Acids." CHIMIA International Journal for Chemistry 75, no. 6 (June 30, 2021): 530–34. http://dx.doi.org/10.2533/chimia.2021.530.

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More than 50% of proteinogenic amino acid sidechains can bind metal ions, enabling proteins and peptides to bear these ions as cofactors. Nevertheless, post-translational modifications and incorporation of noncanonical amino acids bestow peptides and proteins myriads of other coordination capabilities, thanks to an enhanced metal binding. Here we summarize selected examples of natural and artificial systems that contain one or more noncanonical amino acids coordinating a metal ion and subsequently achieve a new or enhanced function. We report on a wide array of systems: from disease-related proteins that undergo sulfurylation or phosphorylation through natural metallophores that selectively capture precious essential ions to synthetic selfassembly strategies, biocatalysts, and chelating agents against toxic metals. Regardless of their (bio)synthetic routes, all possess unique metal-binding properties that could not be effectively achieved by systems composed of canonical residues.

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38

Morozova, Olga V., Olga N. Volosneva, Olga A. Levchenko, Nikolay A. Barinov, and Dmitry V. Klinov. "Protein Corona on Gold and Silver Nanoparticles." Materials Science Forum 936 (October 2018): 42–46. http://dx.doi.org/10.4028/www.scientific.net/msf.936.42.

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Gold or silver nanoparticles (NP) were covered with protein corona by: 1) direct binding with a number of proteins; 2) nanoprecipitation of proteins from their solutions in fluoroalcohols; 3) physisorption of proteins on the NP surface treated with poly (allylamine) s; 4) encapsulation of Ag or Au NP into SiO2 envelope and functionalization with organosilanes. Adsorption of proteins on surfaces of metal NP is reversible and up to 70% of the attached proteins can be eluted. Ag NP possess high affinity for binding with immunoglobulins and fibrinogens but not with any protein. Nanoprecipitation of Ag and Au NP with proteins resulted in combined NP with metal core and protein shell with ligand-binding and enzymatic activities. SiO2 layer on surfaces of metal NP is suitable for silanization and covalent immobilization of any protein. Protein corona prevents Ag and Au NP from oxidation, dissolution and aggregation. Proteins attached to metal NP reduce their antimicrobial activity and cytotoxicity for eukaryotic cells. The developed methods of fabrication of Ag/Au NP with protein shells permit to attach any protein at different distances from metal core to avoid possible inactivation of proteins, to reduce fluorescence fading and to stabilize the nanoconjugates.

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39

Lin, Yanchun, and Michael L. Gross. "Mass Spectrometry-Based Structural Proteomics for Metal Ion/Protein Binding Studies." Biomolecules 12, no. 1 (January 15, 2022): 135. http://dx.doi.org/10.3390/biom12010135.

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Metal ions are critical for the biological and physiological functions of many proteins. Mass spectrometry (MS)-based structural proteomics is an ever-growing field that has been adopted to study protein and metal ion interactions. Native MS offers information on metal binding and its stoichiometry. Footprinting approaches coupled with MS, including hydrogen/deuterium exchange (HDX), “fast photochemical oxidation of proteins” (FPOP) and targeted amino-acid labeling, identify binding sites and regions undergoing conformational changes. MS-based titration methods, including “protein–ligand interactions by mass spectrometry, titration and HD exchange” (PLIMSTEX) and “ligand titration, fast photochemical oxidation of proteins and mass spectrometry” (LITPOMS), afford binding stoichiometry, binding affinity, and binding order. These MS-based structural proteomics approaches, their applications to answer questions regarding metal ion protein interactions, their limitations, and recent and potential improvements are discussed here. This review serves as a demonstration of the capabilities of these tools and as an introduction to wider applications to solve other questions.

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40

Dudev, Todor, and Carmay Lim. "Effect of Carboxylate-Binding Mode on Metal Binding/Selectivity and Function in Proteins." Accounts of Chemical Research 40, no. 1 (January 2007): 85–93. http://dx.doi.org/10.1021/ar068181i.

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41

BERG, J. M. "ChemInform Abstract: Metal-Binding Domains in Nucleic Acid-Binding and Gene-Regulatory Proteins." ChemInform 22, no. 12 (August 23, 2010): no. http://dx.doi.org/10.1002/chin.199112360.

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42

Sano, D., K. Myojo, and T. Omura. "Heavy metal-binding proteins from metal-stimulated bacteria as a novel adsorbent for metal removal technology." Water Science and Technology 53, no. 6 (March 1, 2006): 221–26. http://dx.doi.org/10.2166/wst.2006.200.

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Water pollution with toxic heavy metals is of growing concern because heavy metals could bring about serious problems for not only ecosystems in the water environment but also human health. Some metal removal technologies have been in practical use, but much energy and troublesome treatments for chemical wastes are required to operate these conventional technologies. In this study, heavy metal-binding proteins (HMBPs) were obtained from metal-stimulated activated sludge culture with affinity chromatography using copper ion as a ligand. Two-dimensional electrophoresis revealed that a number of proteins in activated sludge culture were recovered as HMBPs for copper ion. N-termini of five HMBPs were determined, and two of them were found to be newly discovered proteins for which no amino acid sequences in protein databases were retrieved at more than 80% identities. Metal-coordinating amino acids occupied 38% of residues in one of the N-terminal sequences of the newly discovered HMBPs. Since these HMBPs were expected to be stable under conditions of water and wastewater treatments, it would be possible to utilize HMBPs as novel adsorbents for heavy metal removal if mass volume of HMBPs can be obtained with protein cloning techniques.

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43

Tahir, H., M. Misran, M. R. Othman, and N. N. Ibrahim. "Metal Selectivity of Hevea Protein Isolated from Natural Rubber Latex Skim Serum." International Journal of Engineering & Technology 7, no. 4.14 (December 24, 2019): 426. http://dx.doi.org/10.14419/ijet.v7i4.14.27710.

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Hevea protein isolated from skim serum, a by-product of centrifugation process, contains useful proteins in extracting metal. It can be used directly from the source or purified before reacting with metal solutions. Those proteins bind with metal at varying degrees. Upon exposure from as low as 2 ppm concentration to up to 20 ppm metal solution concentration, different binding characteristics were seen. The reasons of such inconsistency in the characteristics might be due to the existence of some of the metal itself in the NRL serum. Mg++ and Zn++ are common metal found in NRL products and those metals would show the slightest in binding with hevea protein. Other metals which were covered in this scope of study shows a good binding characteristics disregard of the group of metals belongs. Selectivity was measured from the final concentration of metal in percentage. In most cases, lead, copper and cadmium show good interaction with hevea proteins.

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44

Fang, Caiyun, Lei Zhang, Xiaoqin Zhang, and Haojie Lu. "Selective enrichment of metal-binding proteins based on magnetic core/shell microspheres functionalized with metal cations." Analyst 140, no. 12 (2015): 4197–205. http://dx.doi.org/10.1039/c5an00599j.

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45

Antsuki, T., D. Sano, and T. Omura. "Functional metal-binding proteins by metal-stimulated bacteria for the development of an innovative metal removal technology." Water Science and Technology 47, no. 10 (May 1, 2003): 109–15. http://dx.doi.org/10.2166/wst.2003.0551.

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Heavy metal pollution has become an environmental problem throughout the world because heavy metals can be accumulated into the food chain and bring about serious problems, not only for ecosystems but also for human health. In this study, functional metal-binding proteins (FMBPs) were isolated from a metal-stimulated activated sludge culture with the aim of applying them to an innovative metal removal technology. Activated sludge bacteria was cultured in growth media including copper ion, and the stimulation of protein production by copper ion led to the 14% increase in a quantity of extracted crude proteins per 1 g of bacterial cell pellet (wet). In order to isolate FMBPs, extracted crude proteins were applied to the immobilized metal affinity column in which each of copper, nickel and zinc was used as a ligand. Several FMBPs were succesfully isolated from copper-stimulated bacteria. One of FMBPs (molecular weight of about 40 kDa) exhibited an ability to adsorb all three metals. The multi metal-binding property of this FMBP could be applied to an innovative metal removal technology. Furthermore, isolated FMBPs that could capture only one kind of heavy metal would also be attractive as a metal adsorbent in recovering a specific metal as a resource from wastewater, including several heavy metals.

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46

Dudev, Todor. "Modeling Metal Binding Sites in Proteins by Quantum Chemical Calculations." Computational Chemistry 02, no. 02 (2014): 19–21. http://dx.doi.org/10.4236/cc.2014.22003.

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47

Andersen, Rolf, John Frazier, and P. C. Huang. "Transition Metal-Binding Proteins from Three Chesapeake Bay Fish Species." Environmental Health Perspectives 65 (March 1986): 149. http://dx.doi.org/10.2307/3430175.

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48

Nakamura, Kensuke, Aki Hirai, Md Altaf-Ul-Amin, and Hiroki Takahashi. "MetalMine: a database of functional metal-binding sites in proteins." Plant Biotechnology 26, no. 5 (2009): 517–21. http://dx.doi.org/10.5511/plantbiotechnology.26.517.

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49

CAMPBELL, JOANNE A., J. DENIS BIGGART, and ROBERT J. ELLIOTT. "Isolation of calcium- binding proteins by immobilized metal affinity chromatography." Biochemical Society Transactions 19, no. 4 (November 1, 1991): 387S. http://dx.doi.org/10.1042/bst019387s.

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50

Andersen, R., J. Frazier, and P. C. Huang. "Transition metal-binding proteins from three Chesapeake Bay fish species." Environmental Health Perspectives 65 (March 1986): 149–56. http://dx.doi.org/10.1289/ehp.8665149.

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