Abstract
X-ray-based techniques are extremely versatile and can provide information regarding the atomic arrangement of atoms in a molecule and are often the method of choice for exploring the structures of proteins and their ligands. The photosynthetic splitting of water and evolution of molecular oxygen by plants and cyanobacteria is one of the key reactions in nature, which is catalysed by a metal site in a membrane-bound photosynthetic protein complex. In this article, we will describe how X-ray pulse lasers can simultaneously probe the overall atomic structure of the photosynthetic system and the electronic structure of a catalytic metal site under physiological conditions in real time.
Highlights
Metal cofactors are integral to the function of many enzymes
X-ray-based techniques have been methods of choice to look at molecular structures of protein complexes and their assemblies
The patterns of diffracted X-rays from crystals can give us information about the atomic arrangement in the proteins
Summary
Metal cofactors are integral to the function of many enzymes. In such metalloenzymes, the metal, frequently from the 3d block of transition metals, serves as the site where various chemical reactions such as electron transfer and catalysis take place. Emission processes can be used as a fingerprint of the chemical state of the metal site Can we combine these two powerful methods, X-ray crystallography and X-ray spectroscopy, for the study of metalloenzymes to simultaneously obtain the overall protein structure and the local electronic structure at the active centre (Figures 2 and 3)? We describe how optical pump pulses to start the reaction and the ultrafast, ultra-bright XFEL pulses can be used to simultaneously probe the overall atomic structure and the active site electronic structure of photosynthetic systems under physiological conditions, and in real time These experiments are examples of a changing paradigm of how to study the structure and function of metalloenzymes
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