Cysteine preparation

CJH4O5, H02CCH(0H)C02H. Colourless crystals with IH O lost at 60 C. M.p. IhO C (decomp.). Prepared by heating dinitrotartaric acid in aqueous alcohol, taurine, aminoethylsulpbonic acid, C2H7NO3S, NHj CHj CH SOjH. Crystallizes in columns, decomposing at 317 C. In combination with cholic acid it forms one of the bile acids. It is formed in the liver from cysteine. 

Permanent coloration can also be achieved by exposing hair to certain metals copper, silver, and especially lead salts. Preparations containing aqueous solutions of lead acetate may include a source of sulfur, usually thiosulfate, which may react with cystine in the hair to produce some cysteine or may react directiy with the metal ion to form dark metallic sulfides. Preparations of this type, which darken hair gradually, are not universally considered safe. 

The Dim ester was developed for the protection of the carboxyl function during peptide synthesis. It is prepared by transesterification of amino acid methyl esters with 2-(hydroxymethyl)-l,3-dithiane and Al(/-PrO)3 (reflux, 4 h, 75°, 12 torr, 75% yield). It is removed by oxidation [H2O2, (NH4)2Mo04 pH 8, H2O, 60 min, 83% yield]. Since it must be removed by oxidation it is not compatible with.sulfur-containing amino acids such as cysteine and methionine. Its suitability for other, easily oxidized amino acids (e.g., tyrosine and tryptophan) must also be questioned. It is stable to CF3CO2H and HCl/ether. - ... 

Thiazolidines have been prepared from /3-aminothiols—for example, cysteine—to protect the —SH and — NH groups during syntheses of peptides, including glu-tathione. Thiazolidines are oxidized to symmetrical disulfides with iodine they do not react with thiocyanogen in a neutral solution. 

A number of 5-sulfenylthiocarbonates have been prepared to protect thiols. A benzyl derivative, R =CH2Ph, is stable to trifluoroacetic acid (25°, 1 h), but not to HBr/AcOH, and provides satisfactory protection during peptide syntheses a t-butyl derivative, R = t-Bu, is too labile in base to provide protection. A methyl derivative, R =CH3, has been used to protect a cysteine fragment that is subsequently converted to a cystine. ... 

These sulfides are prepared from other sulfur-protected cysteine derivatives by reaction with the sulfenyl chloride, The Npys group can also be introduced directly by treatment of the thiol with NpysCl, ... 

Reactions between A -(l-chloroalkyl)pyridinium chlorides 33 and amino acids in organic solvents have a low synthetic value because of the low solubility of the amine partner. A special protocol has been designed and tested in order to circumvent this drawback. Soon after the preparation of the salt, an aqueous solution of the amino acid was introduced in the reaction medium and the two-phase system obtained was heated under reflux for several hours. However, this was not too successful because sulfur dioxide, evolved during the preparation of the salt, was converted into sulfite that acted as an 5-nucleophile. As a result, A -(l-sulfonatoalkyl)pyridinium betaines such as 53 were obtained (Section IV,B,3) (97BSB383). To avoid the formation of such betaines, the salts 33 were isolated and reacted with an aqueous solution of L-cysteine (80) to afford thiazolidine-4-carboxylic acids hydrochlorides 81 (60-80% yields). 

Nakajima and Okawa prepared cysteine (250 Scheme 3.92) by treating aziridine 127a with dry H2S gas in the presence of a catalytic amount of BF3 Et20 [141]. The resulting thiol 248 was then oxidized with iodine to afford disulfide 249 in 70% overall yield. Removal of the Cbz protecting group afforded cysteine (250). 

Figure 10.1 Conformation of epothilone D bound in the P450epol< active site. The figure was prepared from PDB entry 1PKF using Swiss-PdbViewer [27]. The heme prosthetic group is shown with its cysteinate ligand (Cys365) bound. For clarity, amino acids lining the active site have been omitted apart from Phe96.

Relatively few reports have been published subsequently on the use of these reagents. Hope and coworkers99 have used sodium in liquid ammonia to cleave the benzyl sulphonyl derivatives of cysteamine, L-cysteine and L-homocysteine to prepare the corresponding sulphinic acids, as in equation (42). 

The macrocyclization of a peptide was carried out by nucleophihc substitution on a fluorobenzene by the sulfide group of the terminal cysteine of a pentapeptide [164]. The peptide 261 was prepared by standard SPPS and was cyclized under microwave irradiation at 50 °C for 10 min in DMF (Scheme 96). The yields of 262, after cleavage with TFA, were remarkably high for a macrocyclic peptide (70%) and also the resulting HPLC purity was very high. 

Oluwatobi, S. O. and Revaprasadu, N. (2007). A Novel Method to Prepare Cysteine Capped Cadmium Selenide Nanoparticles. Mater. Res. Soc. Symp. Proc. 0951, E03-12. 

In 1984, the first methanogenic CODH was isolated from Methano-sarcina barkeri (138) and was shown to consist of a complex of the a and e subunits, with an apparent molecular mass of 232 kDa. Similar results have been found for other methanogenic CODH preparations (139-143). CODH activity must reside in the a subunit of the methanogenic enzyme, since the e subunit lacks cysteine residues and could... 

Using a combination of techniques such as EPR, resonance Raman, and MCD spectroscopy, the conversion of [2Fe-2S] into [4Fe—4S] centers has been found to take place under reducing conditions in E. coli biotin synthase 281). The as-prepared form of this enzyme has been thought to contain one [2Fe-2S] center per monomer, coordinated by the three cysteine residues of the motif Cys-X3-Cys-X2-Cys and by a fourth, noncysteinyl ligand. Upon reduction, a [4Fe-4S] cluster bridging two monomers may be formed in the active enzyme. In the reduced state, the [4Fe-4S] center is characterized by a mixture of S = I and S = k spin states giving EPR features at g 5.6 and... 

The present procedure provides a convenient method for preparing S-acetamidomethyl-L-cysteine hydrochloride." The zwitterionic form may be obtained readily from the hydrochloride by... 

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