Methionine metal complexes

Methanol, JV-methyIumdazol-2-yldi pyrid-2-yl)-, 88 metal complexes, 89 Methionine metal complexes, 749 Methyleneamido complexes transition metal, 125,129 bonding, 127 reactions, 128 spectroscopy, 128 structures, 127,128 synthesis, 126... 

Methanol,, Y-methylimidazol-2-yldi(pyrid-2-yl)-. 2. ° metal complexes, 2, 89 Methanosarcina bryantii nickel, 6, 645 Methemerythrin, 4, 254 Methemocyanin. 6, 692 eopper(II) complexes, 5, 724 Methionine... 

The closely related dichloroethylenediamine platinum(II) was found to be slightly better than PtCll- as a heavy atom. A platinum-sulphur bond to methionine 29 is formed according to current analysis (now confirmed). The platinum cannot be removed by washing the crystal in sharp contrast to the reversible binding of other metal complexes. ... 

The LFMM FF for the oxidized Cu(II) centers was designed around suitable homoleptic species, viz., [Cu(imidazole)4]2+, [Cu(SCH3)4]2-, [Cu(S(CH3)2)4]2+, and [Cu(0=CH2)4]2+ (37). These complexes represent models for Cu-histidine, Cu-cysteine, Cu-methionine, and Cu-glutamine O/peptide respectively. Only the first of these species is known experimentally. However, it is amply documented that DFT gives excellent structures for metal complexes (64,65) so we can access the remaining species computationally (Fig. 20). 

Keywords Alpha-amylase complex. Amino acid acylase. Acetyl methionine. Metal ions and Ninhydrin. 

Several types of donor-acceptor pairs were used tyrosine-tryptophan, methionine-tyrosine and pairs of metal complexes. Spacer was specially designed peptides. 

McAuliffe et al. studied the IR spectra of metal complexes of methionine [CH,—S—CH,—CH2—CH(NH2)—COOH). They found lhat most of the metals they studied [except Ag(l)] coordinate through the NHj and COO ... 

Ru(tap)J (complex 2) of DL-methionine, and complex 1 is shown in Figure 1. The composition of 2 in solution was determined by Job s method of continuous variation and the metal ligand ratio was found to be 2 1. The pH of the solution was adjusted by adding NaOH/HClO, and the measurements were carried out with the help of a Sartorius make digital pH meter (PB 11) with an accuracy of 0.01 unit. 

The metalloproteins consist of a metal complex imbedded in and bonded to a protein net of covalently bonded amino acids. The most commonly studied systems are the myoglobins and cytochromes, which contain Fe(II) or Fe(III) in a porphyrin complex, or the copper blue proteins, which have Cu(II) or Cu(I) compiexed most often by histidine nitrogens and cysteine and methionine sulfurs from the protein. Metalloproteins can be oxidized or reduced by standard transition-metal complex reagents, and the latter usually are chosen to ensure outer-sphere electron transfer. This area has been the subject of numerous reviews. 

Severin etal recently pnblished another successful array for differentiating peptides by employing three commercially available metal complexes (27-29). One complex contained rhodium, one ruthenium, and one palladium. In the presence of six selected fluorophores, these constituents formed a collection of differential sensors. The receptors were able to differentiate 10 dipeptides at a 50 pM concentration (the closed symbols in Figure 9) and 2 dipeptides at 20 pM concentration (the open symbols in Figure 9). The authors found that peptides containing histidine and methionine residues were best discriminated, most likely because these residues displaced a larger fraction of... 

Column 3 RNA species. RNAs and pol mucleotides arranged alphabetically under each metal oxidation state and metal complex first by polyribonucleotide species, then by tRNA species in order of amino acid and then source organism, mixed (unfractionated) species listed after those identified by amino acid, and finally by RNA species other than tRNAs. Amino acids are abbreviated by the three letter nomenclature, Ala , Arg , etc. Met P and Met m .represent the translational initiator and the ordinary methionine spedes, respectively. TYMV=turnip yellow mosaic virus. TMV=tobacco mosaic virus. 

McLafferty rearrangement 133, 163 Meisenheimer complexes 699, 702 Metal-chelated intermediates 838 Metal-halogen exchange 781, 784 Methionine, oxidation of 852-855 Methionine sulphone 853 Methionine sulphoxide 851-869 reduction of 1063 residues of... 

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