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Homolytic Cleavage (homolytic + cleavage)
Selected AbstractsAn investigation of the homolytic saccharide cleavage of deprotonated flavonol 3- O -glycosides in a quadrupole ion trap mass spectrometerJOURNAL OF MASS SPECTROMETRY (INCORP BIOLOGICAL MASS SPECTROMETRY), Issue 8 2008Barry D. Davis Abstract The trend in the extent of homolytic saccharide cleavage is reported for a series of deprotonated flavonol 3- O -glycosides upon collision-induced dissociation (CID) in a quadrupole ion trap mass spectrometer. The second-generation product ions from the primary [Y0], and [Y0, H],, product ions were also identified. It was determined that the structure of both the aglycon and the saccharide portions of the flavonoid glycoside are pivotal in inducing radical cleavage. In contrast to earlier work on this subject reported for a smaller group of flavonols, the correlation between the degree of B-ring hydroxylation and the extent of radical saccharide cleavage showed several notable exceptions in the present work. Homolytic cleavage was also investigated in the context of using tandem mass spectrometry to identify the aglycon portions of flavonoid glycosides. Copyright © 2008 John Wiley & Sons, Ltd. [source] Gas-phase radical,radical recombination reactions of nitroxides with substituted phenyl radicalsINTERNATIONAL JOURNAL OF CHEMICAL KINETICS, Issue 4 2004J. L. Heidbrink Fourier-transform ion cyclotron resonance mass spectrometry has been used to examine gas-phase reactions of four different nitroxide free radicals with eight positively charged pyridyl and phenyl radicals (some containing a Cl, F, or CF3 substituent). All the radicals reacted rapidly (near collision rate) with nitroxides by radical,radical recombination. However, some of the radicals were also able to abstract a hydrogen atom from the nitroxide. The results establish that the efficiency (kreaction/kcollision) of hydrogen atom abstraction varies with the electrophilicity of the radical, and hence is attributable to polar effects (a lowering of the transition-state energy by an increase in its polar character). The efficiency of the recombination reaction is not sensitive to substituents, presumably due to a very low reaction barrier. Even so, after radical,radical recombination has occurred, the nitroxide adduct was found to fragment in different ways depending on the structure of the radical. For example, a cationic fragment was eliminated from the adducts of the more electrophilic radicals via oxygen anion abstraction by the radical (i.e., the nitroxide adduct cleaves heterolytically), whereas adducts of the less electrophilic radicals predominantly fragmented via homolytic cleavage (oxygen atom abstraction). Therefore, differences in the product branching ratios were found to be attributable to polar factors. © 2004 Wiley Periodicals, Inc. Int J Chem Kinet 36: 216,229 2004 [source] Thermally induced intramolecular oxygen migration of N -oxides in atmospheric pressure chemical ionization mass spectrometryRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 19 2010Xin Wang N -Oxides are known to undergo three main thermal degradation reactions, namely deoxygenation, Cope elimination (for N -oxides containing a ,-hydrogen) and Meisenheimer rearrangement, in atmospheric pressure chemical ionization mass spectrometry (APCI-MS). The ions corresponding to these thermal degradants observed in the ensuing APCI mass spectra have been used to identify N -oxides as well as to determine the N -oxidation site when the analyte contains multiple tertiary amine groups. In this paper, we report a thermally induced oxygen migration from one N -oxide amine to another tert -amine group present in the same molecule through a six-membered ring transition state during APCI-MS analysis. The observed intramolecular oxygen migration resulted in the formation of a new isomeric N -oxide, rendering the results of the APCI-MS analysis more difficult to interpret and potentially misleading. In addition, we observed novel degradation behavior that happened after the Meisenheimer rearrangement of the newly formed N -oxide: a homolytic cleavage of the NO bond instead of elimination of an aldehyde or a ketone that usually follows the rearrangement. Understanding of these unusual degradation pathways, which have not been reported previously, should facilitate structural elucidation of N -oxides using APCI-MS analysis. Copyright © 2010 John Wiley & Sons, Ltd. [source] Electron ionisation mass spectral studies of bridgehead-fused ,2 -norbornanethiazolinesRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 6 2009Antonio García Martínez The electron ionisation (EI) mass spectra of a series of bridgehead-fused ,2 -norbornanethiazolines, a new class of bridgehead-norbornane derivatives, have been studied and their cleavage mechanisms rationalised on the basis of the substituent shifts as well as on the identification of relevant peaks through accurate mass measurements and collision-induced dissociation tandem mass spectrometric experiments. The fragmentation patterns of isomeric pairs of 6,6- and 10,10-dimethylnorbornanethiazolines are almost identical, probably due to an initial isomerisation of molecular ion previous to the fragmentation. In general, the dominant peaks in the spectra of all the studied compounds originate from initial , -cleavages of C(5),C(6) or C(1),C(10) bonds, followed by concomitant homolytic cleavage of C(1),C(9) and C(7),C(10) bonds. The driving force for this fragmentation pathway, directed by the gem -dimethyl group, is the formation of a highly stabilised thiazolilmethyl cation which constitutes the base peak in all the spectra and allows the identification of these interesting ligands. Copyright © 2009 John Wiley & Sons, Ltd. [source] Adenosyl Radical: Reagent and Catalyst in Enzyme ReactionsCHEMBIOCHEM, Issue 5 2010E. Neil G. Marsh Prof. Abstract Adenosine is undoubtedly an ancient biological molecule that is a component of many enzyme cofactors: ATP, FADH, NAD(P)H, and coenzyme A, to name but a few, and, of course, of RNA. Here we present an overview of the role of adenosine in its most reactive form: as an organic radical formed either by homolytic cleavage of adenosylcobalamin (coenzyme B12, AdoCbl) or by single-electron reduction of S -adenosylmethionine (AdoMet) complexed to an iron,sulfur cluster. Although many of the enzymes we discuss are newly discovered, adenosine's role as a radical cofactor most likely arose very early in evolution, before the advent of photosynthesis and the production of molecular oxygen, which rapidly inactivates many radical enzymes. AdoCbl-dependent enzymes appear to be confined to a rather narrow repertoire of rearrangement reactions involving 1,2-hydrogen atom migrations; nevertheless, mechanistic insights gained from studying these enzymes have proved extremely valuable in understanding how enzymes generate and control highly reactive free radical intermediates. In contrast, there has been a recent explosion in the number of radical-AdoMet enzymes discovered that catalyze a remarkably wide range of chemically challenging reactions; here there is much still to learn about their mechanisms. Although all the radical-AdoMet enzymes so far characterized come from anaerobically growing microbes and are very oxygen sensitive, there is tantalizing evidence that some of these enzymes might be active in aerobic organisms including humans. [source] | ||||||||||