Amino acids dissolving metals

Another variation involves the stripping or electrolysis of species that have spontaneously adsorbed on the surface of an electrode without the preelectrolysis step. This technique, called adsorptive stripping voltammetry, can be applied, for example, to sulfur-containing species, organic compounds, and certain metal chelates that adsorb on Hg and Au (74, 81). Examples include cysteine (and proteins that contain this amino acid), dissolved titanium in the presence of the chelator solochrome violet RS, and the drug diazepam. The amounts found by this method would necessarily be limited to monolayer levels. However, similar approaches can be employed with thicker polymer layers that can interact with solution species. Related experiments are described in Chapter 14. 

Because of their zwitterionic nature, amino acids are generally soluble in water. Their solubility in organic solvents rises as the fat-soluble portion of the molecule increases. The likeliest impurities are traces of salts, heavy metal ions, proteins and other amino acids. Purification of these is usually easy, by recrystallisation from water or ethanol/water mixtures. The amino acid is dissolved in the boiling solvent, decolorised if necessary by boiling with Ig of acid-washed charcoal/lOOg amino acid, then filtered hot, chilled, and set aside for several hours to crystallise. The crystals are filtered off, washed with ethanol, then ether, and dried. 

It is believed that nickel penetrates the skin and acts as a hapten, complexing with selected peptide and/or amino-acid ligands to distort intercellular or cellular proteins, stimulating a type IV delayed (cell-mediated) hypersensitivity reaction [398]. Nickel water-soluble salts, like nickel chloride and nickel sulphate, are strong sensitizers [213, 215], The chloride induced in sweat is apparently an important factor in dissolving the metallic nickel, permitting the soluble nickel salts to act. 

Rate-determining step, hydroformylation, 163 Reactivity, enantiomers, 286 Recognition, enantiomers, 278 Reduction and oxidation, 5 Reductive coupling, dissolving metal, 288 Reductive elimination, 5, 111 Resolution. See Kinetic resolution Rhenium-carbene complexes, 288 Rhodium-catalyzed hydrogenation, 17, 352 amino acid synthesis, 18, 352 BINAP, 20... 

After adsorption one side of the protein molecule is oriented towards the sorbent surface, turned away from the aqueous solution. As a consequence, hydrophobic parts of the protein that are buried in the interior of the dissolved molecule may become exposed to the sorbent surface where they are still shielded from contact with water. Because hydrophobic interaction between apolar amino acid residues in the protein s interior support the formation of secondary structures as a-helices and P-sheets, a reduction of this interaction destabilizes such structures. Breakdown of the a-helices and/or P-sheets content is, indeed, expected to occur if peptide units released from these ordered structures can form hydrogen bonds with the sorbent surface. This is the case for polar surfaces such as oxides, e.g. silica and metal oxides, and with sorbent retaining residual water at their surfaces. Then the decrease in ordered secondary structures leads to an increased conformational entropy of the protein. This may favour the protein adsorption process considerably.13 It may be understood that proteins having an intrinsically low structural stability are more prone to undergo adsorption-induced structural changes. 

Chen, Z. and Mayer, L.M., Sedimentary metal bioavailability determined by the digestive constraints of marine deposit feeders Gut retention time and dissolved amino acids, Mar. Ecol.-Prog. Ser., 176, 139, 1999. 

---