S Beranová

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The internal energy distributions P(ε) transferred to W(CO) 6 (+·) during the kiloelectronvolt collisions that occur upon neutralization-reionization (NR) have been estimated based on the relative abundances of the W(CO) 0-6 (+·) products present in NR spectra (thermochemical method). The average internal energy of the incipient {W(CO) 6 (+·) }(*) ions(More)
Inactivation of the enzyme L-aspartase from Escherichia coli by the substrate analog aspartate beta-semialdehyde has previously been shown to occur by the mechanism-based conversion to the corresponding product aldehyde, followed by covalent modification of cysteine-273 (F. Giorgianni et al. (1995) Biochemistry 34, 3529). Inactivation by the product analog,(More)
The catalytic activity of the enzyme L-aspartase from Escherichia coli has previously been shown to be sensitive to sulfhydryl reagents. The use of group-specific reagents, and a sequence homology comparison study among the fumarase-aspartase family of enzymes, has not, however, lead to the identification of a specific, essential cysteinyl residue. We have(More)
The neutral species eliminated upon fragmentation of fast-moving mass-selected ions can be directly identified by collisional ionization and detection in neutral fragment reionization (Nf R) mass spectra. Establishment of the identity of neutral fragments yields valuable insight into the decomposition mechanism of a precursor ion, as demonstrated for(More)
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