. (2015) 'Excited state dynamics of the isolated green uorescent protein chromophore anion following UV excitation.', Journal of physical chemistry B., 119 (10). pp. 3982-3987. Further information on publisher's website:http://dx.doi.org/10.1021/acs.jpcb.5b01432Publisher's copyright statement:This document is the Accepted Manuscript version of a Published Work that appeared in nal form in The Journal of Physical Chemistry B, copyright c American Chemical Society after peer review and technical editing by the publisher. To access the nal edited and published work see http://dx.doi.org/10.1021/acs.jpcb.5b01432. Additional information:Use policyThe full-text may be used and/or reproduced, and given to third parties in any format or medium, without prior permission or charge, for personal research or study, educational, or not-for-pro t purposes provided that:• a full bibliographic reference is made to the original source • a link is made to the metadata record in DRO • the full-text is not changed in any way The full-text must not be sold in any format or medium without the formal permission of the copyright holders.Please consult the full DRO policy for further details.

The anionic form of p-hydroxybenzylidene-2,3-dimethylimidazolinone (HBDI) has been extensively employed as a model of the chromophore of the green fluorescence protein. The bright S1 excited state HBDI(-) has a measured lifetime of 1.4 ps in the gas-phase and is dominated by two non-radiative decay mechanisms: internal conversion and autodetachment into the neutral continuum. Here, time-resolved photoelectron spectroscopy has been used to determine the yields of these two channels from which the lifetime for autodetachment was found to be ∼30 ps.

Herein we report a practical synthetic route to the lasso peptide lassomycin () and C-terminal variant lassomycin-amide (). The biological evaluation of peptides and against Mycobacterium tuberculosis revealed that neither had any activity against this bacterium. This lack of biological activity has led us to propose that naturally occurring lassomycin may actually exhibit a standard lasso peptide threaded conformation rather than the previously reported unthreaded structure.

Graphical abstractHerein, a series of aromatic pentafluorosulfanyl (SF5) containing amino acids are reported. A Negishi cross-coupling strategy utilising a catalyst system of Pd(dba)2 and SPhos afforded the aforementioned SF5 amino acids in yields between 35% and 42%. Two dipeptides utilising both the amine and carboxylic functionalities of the synthesised SF5 containing amino acids were prepared, demonstrating their compatibility with common amide/peptide coupling reagents and strategies.