2 resultados para Reactive species of oxygen

em CaltechTHESIS


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A series of terl-butylperoxide complexes of hafnium, Cp*2Hf(R)(OOCMe3) (Cp* = ((η5-C5Me5); R = Cl, H, CH3, CH2CH3, CH2CH2CH3, CH2CH2CH2CH3, CH2CHMe2, CH=CHCMe3, C6H5, meta-C6H3(CH2)2) and Cp*(η5-C5(CH3)4CH2CH2CH2)Hf(OOCMe3), has been synthesized. One example has been structurally characterized, Cp*2Hf(OOCMe3)CH2CH3 crystallizes in space group P21/c, with a = 19.890(7)Å, b = 8.746(4)Å, c = 17.532(6)Å, β = 124.987(24)°, V = 2498(2)Å3, Z = 4 and RF = 0.054 (2222 reflections, I > 0). Despite the coordinative unsaturation of the hafnium center, the terl-butylperoxide ligand is coordinated in a mono-dentate ligand. The mode of decomposition of these species is highly dependent on the substituent R. For R = H, CH2CH3, CH2CH2CH3, CH2CH2CH2CH3, CH2CHMe2 a clean first order conversion to Cp*2Hf(OCMe3)(OR) is observed (for R CH2CH3, ΔHǂ = 19.6 kcal•mol-1, ΔSǂ = -13 e.u.). These results are discussed in terms of a two step mechanism involving η2-coordination of the terl-butylperoxide ligand. Homolytic O-O bond cleavage is observed upon heating of Cp*2Hf(OOCMe3) R (R = C6H6, meta-C6H3(CH3)2). In the presence of excess 9,10-dihydroanthracene thermolysis of Cp*2Hf(OOCMe3)C6H6 cleanly affords Cp*2Hf(C6H6)OH and HOCMe3 (ΔHǂ = 22.6 kcal•mol-1, ΔSǂ = -9 e.u.). The O-O bond strength in these complexes is thus estimated to be 22 kcal•mol-1.

Cp*2Ta(CH2)H, Cp*2Ta(CHC6H5)H, Cp*2Ta(C6H4)H, Cp*2Ta(CH2=CH2)H and Cp*2Ta(CH2=CHMe)H react, presumably through Cp*2Ta-R intermediates, with H2O to give Cp*2Ta(O)H and alkane. Cp*2Ta(O)H was structurally characterized: space group P21/n, a= 13.073(3)Å, b = 19.337(4)Å, c = 16.002(3)Å, β = 108.66(2)°, V = 3832(1)Å3, Z = 8 and RF = 0.0672 (6730 reflections). Reaction of terlbutylhydroperoxide with these same starting materials ultimately yields Cp*2Ta(O)R and HOCMe3. Cp*2Ta(CH2=CHR)OH species are proposed as intermediates in the olefin hydride reactions. Cp*2Ta(O2)R species can be generated from the reaction of the same starting materials and O2. Lewis acids have been shown to promote oxygen insertion in these complexes.

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The structural specificity of α-chymotrypsin for polypeptides and denatured proteins has been examined. The primary specificity of the enzyme for these natural substrates is shown to closely correspond to that observed for model substrates. A pattern of secondary specificity is proposed.

A series of N-acetylated peptide esters of varying length have been evaluated as substrates of α-chymotrypsin. The results are interpreted in terms of proposed specificity theories.

The α-chymotrypsin-catalyzed hydrolyses of a number of N-acetylated dipeptide methyl esters were studied. The results are interpreted in terms of the available specificity theories and are compared with results obtained in the study of polypeptide substrates. The importance of non-productive binding in determining the kinetic parameters of these substrates is discussed. A partial model of the locus of the active site which interacts with the R’1CONH- group of a substrate of the form R’1CONHCHR2COR’3 is proposed.

Finally, some reactive esters of N-acetylated amino acids have been evaluated as substrates of α-chymotrypsin. Their reactivity and stereo-chemical behavior are discussed in terms of the specificity theories available. The importance of a binding interaction between the carboxyl function of the substrate and the enzyme is suggested by the results obtained.