Spin-alignment and g-factor measurement of the I^{\pi} = 12+ isomer in 192Pb produced in the relativistic-energy fragmentation of a 238U beam

Reactions of a 16.8 MeV ⁶He beam with a ⁹Be target have been investigated using highly segmented detector setup covering a large solid angle. Data on elastic and quasi-free scattering, as well as two-neutron transfer, are reported. The results for elastic scattering are fairly well reproduced by a CDCC calculation, in agreement with the interpretation of a breakup effect already observed for the scattering of ⁶He on other light targets. Exotic quasi-free scattering of ⁶He on $ \alpha$ -cluster in ⁹Be is clearly observed. Inclusive and coincident events were used to extract information on the two-neutron transfer reaction ⁹Be(⁶He, $ \alpha$ )¹¹Be . Sequential decay of the ¹¹Be state at the excitation energy $\ensuremath E_x = 10.6$ MeV through different channels is discussed.     

Structure and Function of the α-Hydroxylation Bimodule of the Mupirocin Polyketide Synthase

Mupirocin is a clinically important antibiotic produced by a trans-AT Type I polyketide synthase (PKS) in Pseudomonas fluorescens. The major bioactive metabolite, pseudomonic acid A (PA−A), is assembled on a tetrasubstituted tetrahydropyran (THP) core incorporating a 6-hydroxy group proposed to be introduced by α-hydroxylation of the thioester of the acyl carrier protein (ACP) bound polyketide chain. Herein, we describe an in vitro approach combining purified enzyme components, chemical synthesis, isotopic labelling, mass spectrometry and NMR in conjunction with in vivo studies leading to the first characterisation of the α-hydroxylation bimodule of the mupirocin biosynthetic pathway. These studies reveal the precise timing of hydroxylation by MupA, substrate specificity and the ACP dependency of the enzyme components that comprise this α-hydroxylation bimodule. Furthermore, using purified enzyme, it is shown that the MmpA KS⁰ shows relaxed substrate specificity, suggesting precise spatiotemporal control of in trans MupA recruitment in the context of the PKS. Finally, the detection of multiple intermodular MupA/ACP interactions suggests these bimodules may integrate MupA into their assembly.