Danqiong Zhu

This book aims to overcome the still prevailing schizophrenic divisions among sciences, humanities, the arts, and multiple forms of ecological knowledge. Discover how these seemingly disparate fields converge to shape the future of biocultural conservation and restoration. The groundbreaking book challenges the traditional divide between the sciences and humanities, offering fresh insights from ecologists, philosophers, artists, and emerging scholars. It is organized into three main parts that address the theory, practice, and communication of biocultural conservation and restoration. The first part presents philosophical concepts and issues that illuminate the ontological, epistemological, aesthetic, and ethical dimensions of biocultural conservation and restoration.. In Part II, a diverse array of art projects from around the world are presented to illuminate the values of biocultural diversity. These initiatives foster deep connections between people and their local environments, often inviting audiences to encounter, observe, touch, and appreciate the often-overlooked biodiversity –such as mosses, lichens, and insects. These artistic endeavours demonstrate that arts can be a powerful tool for communicating the ecological and aesthetic significance of biocultural diversity, and it also is a vital catalyst for positive socio-ecological changes. By engaging communities, these projects contribute to to sustainable biocultural stewardship. In Part III, different chapters emphasize pedagogical and communicative strategies for linking arts to more inclusive biocultural conservation and restoration. By integrating arts and education, this approach enhances biocultural communication. This book is oriented towards a broad public interested in the intersections of environmental issues and the arts. Because of its “interdisciplinary” nature, this volume provides valuable insights that will enhance your understanding and inspire new ideas for innovative collaborations.

© 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.

© 2017 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.X-ray crystallography at X-ray free-electron laser sources is a powerful method for studying macromolecules at biologically relevant temperatures. Moreover, when combined with complementary techniques like X-ray emission spectroscopy, both global structures and chemical properties of metalloenzymes can be obtained concurrently, providing insights into the interplay between the protein structure and dynamics and the chemistry at an active site. The implementation of such a multimodal approach can be compromised by conflicting requirements to optimize each individual method. In particular, the method used for sample delivery greatly affects the data quality. We present here a robust way of delivering controlled sample amounts on demand using acoustic droplet ejection coupled with a conveyor belt drive that is optimized for crystallography and spectroscopy measurements of photochemical and chemical reactions over a wide range of time scales. Studies with photosystem II, the phytochrome photoreceptor, and ribonucleotide reductase R2 illustrate the power and versatility of this method.