Fig. 1: Composition characteristics, local coordination environment and electronic structure of catalyst. | Nature Communications

Fig. 1: Composition characteristics, local coordination environment and electronic structure of catalyst.

From: Axially engineered single atoms in enzyme-mimic-binding pocket steering dehalogenation–polymerization pathways toward water pollutant upcycling

Fig. 1: Composition characteristics, local coordination environment and electronic structure of catalyst.The alternative text for this image may have been generated using AI.

a Overall structure of CYP152 Peroxygenases (POD, P450 BS beta mutant F46A, Protein Data Bank ID: 9IY1). Amino acid fragments act as axial ligands that modulate the oxidative valence of the metal center, facilitating the promotion of oxidant activation, substrate recognition binding and maintenance of enzyme activity. The binding pocket consists of hydrophobic amino acid residues together with amino acid residues involved in polar interactions, providing a favorable microenvironment that not only promotes oxidant activation but also facilitates substrate binding and product release. For the enzyme model, light gray, carbon; red, oxygen; blue, nitrogen; reddish-brown, cobalt; yellow, carbon of the porphyrin ring. b Schematic diagram of catalyst synthesis process. For the model, red, iron; blue, nitrogen; light gray, carbon. c HAADF and EDS Mapping images and d ACHAADF-STEM images of the catalyst. e Atom-overlapping Gaussian-function-fitting mapping of the square and intensity profile along X-Y in (d). f XANES inset: magnification of local areas and fitting of oxidation valence and g FT-EXAFS spectra in R-space of Fe-SACs and reference samples at Fe K-edge. h The ratio IA/IB of the relative strengths of the two Fe K-edge eigenpeaks A and B present at 7132 and 7140 eV reflects the degree of plane distortion in the local environment of monatomic iron. Source data are provided as a Source data file.

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