Inclusive J/psi production in Upsilon decay via color-octet mechanisms

Calculations for inclusive J/psi production in Upsilon decay through the color-octet mechanisms b\bar b[^3S_1, 1] -> c \bar c[^{2s+1}L_J, 8] + g are presented. It is shown that these O(alpha^5_sv^4_c) contributions compete with other color-octet mechanisms considered in the literature. A critical numerical analysis of the color-octet contributions to Upsilon -> J/psi + X shows that further work in this channel, both theoretical and experimental, is necessary in order to clearly understand the significance of the color-octet component of the c \bar c component inside the J/psi system.Comment: Minor changes, corrected typos, version to be published in PR

SUSY Higgs Boson Decays into Scalar Quarks: QCD Corrections

In supersymmetric theories, the decays of the neutral CP-even and CP-odd as well as the charged Higgs bosons into scalar quarks, in particular into top and bottom squarks, can be dominant if they are kinematically allowed. We calculate the QCD corrections to these decay modes in the minimal supersymmetric extension of the Standard Model, including all quark mass terms and squark mixing. These corrections turn out to be rather large, altering the decay widths by an amount which can be larger than 50%. The corrections can be either positive or negative, and depend strongly on the mass of the gluino. We also discuss the QCD corrections to the decays of heavy scalar quarks into light scalar quarks and Higgs bosons.Comment: 17 pages, 6 figure

Structure of a <i>Clostridium botulinum</i> C143S Thiaminase I/Thiamin Complex Reveals Active Site Architecture,

Thiaminases are responsible for the degradation of thiamin and its metabolites. Two classes of thiaminases have been identified based on their three-dimensional structures and their requirements for a nucleophilic second substrate. Although the reactions of several thiaminases have been characterized, the physiological role of thiamin degradation is not fully understood. We have determined the three-dimensional X-ray structure of an inactive C143S mutant of Clostridium botulinum (Cb) thiaminase I with bound thiamin at 2.2 Å resolution. The C143S/thiamin complex provides atomic level details of the orientation of thiamin upon binding to Cb-thiaminase I and the identity of active site residues involved in substrate binding and catalysis. The specific roles of active site residues were probed by using site directed mutagenesis and kinetic analyses, leading to a detailed mechanism for Cb-thiaminase I. The structure of Cb-thiaminase I is also compared to the functionally similar but structurally distinct thiaminase II

Structural basis for antibiotic action of the B1 antivitamin 2′-methoxy-thiamine

The natural antivitamin 2′-methoxy-thiamine (MTh) is implicated in the suppression of microbial growth. However, its mode of action and enzyme-selective inhibition mechanism have remained elusive. Intriguingly, MTh inhibits some thiamine diphosphate (ThDP) enzymes, while being coenzymatically active in others. Here we report the strong inhibition of Escherichia coli transketolase activity by MTh and unravel its mode of action and the structural basis thereof. The unique 2′-methoxy group of MTh diphosphate (MThDP) clashes with a canonical glutamate required for cofactor activation in ThDP-dependent enzymes. This glutamate is forced into a stable, anticatalytic low-barrier hydrogen bond with a neighboring glutamate, disrupting cofactor activation. Molecular dynamics simulations of transketolases and other ThDP enzymes identify active-site flexibility and the topology of the cofactor-binding locale as key determinants for enzyme-selective inhibition. Human enzymes either retain enzymatic activity with MThDP or preferentially bind authentic ThDP over MThDP, while core bacterial metabolic enzymes are inhibited, demonstrating therapeutic potential