Long Pham

The article focuses on the study of workplace learning for hospital’s staff to become mortuary care agents. It is based on the analysis of verbalizations obtained from self-confrontations interviews made with the mortuary care trainees. These interviews are extracted from video recordings taken while trainees carry out their normal task. The goal is to identify, within the context of the interaction between trainees and tutors, signs of learning progress in the trainees’ verbalizations, which could be linked to existing hospital standards. As demonstrated by the activity clinic methodology, these verbalizations are not just a simple depiction of the work activity as it happened but serve as an experiment to underline the learning benefits for the trainees. Beyond the benefits of better understanding the trainees work tasks, the resulting analyses indeed support the formative aspect of self-confrontation interviews. In this perspective, the article focuses on a methodological aspect, the data analysis to account for signs of learning such as verbalized and recognized by the trainees in their interactions with tutors. On the occasion, we question the formative dimension of this methodological setting in the prospect of designing training devices for these professionals.

© 2016 Macmillan Publishers Limited, part of Springer Nature. All rights reserved.Light-induced oxidation of water by photosystem II in plants, algae and cyanobacteria has generated most of the dioxygen in the atmosphere. PS II, a membrane-bound multi-subunit pigment protein complex, couples the one-electron photochemistry at the reaction centre with the four-electron redox chemistry of water oxidation at the Mn 4 CaO 5 cluster in the oxygen-evolving complex. Under illumination, the OEC cycles through five intermediate S-states, in which S 1 is the dark-stable state and S 3 is the last semi-stable state before O-O bond formation and O 2 evolution. A detailed understanding of the O-O bond formation mechanism remains a challenge, and will require elucidation of both the structures of the OEC in the different S-states and the binding of the two substrate waters to the catalytic site. Here we report the use of femtosecond pulses from an X-ray free electron laser to obtain damage-free, room temperature structures of dark-adapted, two-flash illuminated, and ammonia-bound two-flash illuminated PS II. Although the recent 1.95 Å resolution structure of PS II at cryogenic temperature using an XFEL provided a damage-free view of the S 1 state, measurements at room temperature are required to study the structural landscape of proteins under functional conditions, and also for in situ advancement of the S-states. To investigate the water-binding site, ammonia, a water analogue, has been used as a marker, as it binds to the Mn 4 CaO 5 cluster in the S 2 and S 3 states. Since the ammonia-bound OEC is active, the ammonia-binding Mn site is not a substrate water site. This approach, together with a comparison of the native dark and 2F states, is used to discriminate between proposed O-O bond formation mechanisms.