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Instruments / Technical Area	Publication Details	Published
B18-Core EXAFS	Biotechnological synthesis of Pd/Ag and Pd/Au nanoparticles for enhanced Suzuki–Miyaura cross‐coupling activity Richard Kimber , Fabio Parmeggiani , Thomas S. Neill , Mohamed L. Merroun , Gregory Goodlet , Nigel A. Powell , Nicholas J. Turner , Jonathan R. Lloyd Microbial Biotechnology 299 DOI: 10.1111/1751-7915.13762 Diamond Proposal Number(s): [20618] Open Access Show Abstract ▼ Abstract: Bimetallic nanoparticle catalysts have attracted considerable attention due to their unique chemical and physical properties. The ability of metal‐reducing bacteria to produce highly catalytically active monometallic nanoparticles is well known; however, the properties and catalytic activity of bimetallic nanoparticles synthesized with these organisms is not well understood. Here, we report the one‐pot biosynthesis of Pd/Ag (bio‐Pd/Ag) and Pd/Au (bio‐Pd/Au) nanoparticles using the metal‐reducing bacterium, Shewanella oneidensis, under mild conditions. Energy dispersive X‐ray analyses performed using scanning transmission electron microscopy (STEM) revealed the presence of both metals (Pd/Ag or Pd/Au) in the biosynthesized nanoparticles. X‐ray absorption near‐edge spectroscopy (XANES) suggested a significant contribution from Pd(0) and Pd(II) in both bio‐Pd/Ag and bio‐Pd/Au, with Ag and Au existing predominately as their metallic forms. Extended X‐ray absorption fine‐structure spectroscopy (EXAFS) supported the presence of multiple Pd species in bio‐Pd/Ag and bio‐Pd/Au, as inferred from Pd–Pd, Pd–O and Pd–S shells. Both bio‐Pd/Ag and bio‐Pd/Au demonstrated greatly enhanced catalytic activity towards Suzuki–Miyaura cross‐coupling compared to a monometallic Pd catalyst, with bio‐Pd/Ag significantly outperforming the others. The catalysts were very versatile, tolerating a wide range of substituents. This work demonstrates a green synthesis method for novel bimetallic nanoparticles that display significantly enhanced catalytic activity compared to their monometallic counterparts.	Mar 2021
I24-Microfocus Macromolecular Crystallography	Structural analysis and biochemical properties of laccase enzymes from two Pediococcus species Isidoro Olmeda , Patricia Casino , Robert E. Collins , Ramón Sendra , Sara Callejón , Juanjo Huesa , Alexei S. Soares , Sergi Ferrer , Isabel Pardo Microbial Biotechnology 9 DOI: 10.1111/1751-7915.13751 Diamond Proposal Number(s): [14739, 20229] Open Access Show Abstract ▼ Abstract: Prokaryotic laccases are emergent biocatalysts. However, they have not been broadly found and characterized in bacterial organisms, especially in lactic acid bacteria. Recently, a prokaryotic laccase from the lactic acid bacterium Pediococcus acidilactici 5930, which can degrade biogenic amines, was discovered. Thus, our study aimed to shed light on laccases from lactic acid bacteria focusing on two Pediococcus laccases, P. acidilactici 5930 and Pediococcus pentosaceus 4816, which have provided valuable information on their biochemical activities on redox mediators and biogenic amines. Both laccases are able to oxidize canonical substrates as ABTS, ferrocyanide and 2,6‐DMP, and non‐conventional substrates as biogenic amines. With ABTS as a substrate, they prefer an acidic environment and show sigmoidal kinetic activity, and are rather thermostable. Moreover, this study has provided the first structural view of two lactic acid bacteria laccases, revealing new structural features not seen before in other well‐studied laccases, but which seem characteristic for this group of bacteria. We believe that understanding the role of laccases in lactic acid bacteria will have an impact on their biotechnological applications and provide a framework for the development of engineered lactic acid bacteria with enhanced properties.	Feb 2021
I04-1-Macromolecular Crystallography (fixed wavelength)	Characterization and structure-guided engineering of the novel versatile terpene monooxygenase CYP109Q5 from Chondromyces apiculatus DSM436 Jan M. Klenk , Paulina Dubiel , Mahima Sharma , Gideon Grogan , Bernhard Hauer Microbial Biotechnology 12 DOI: 10.1111/1751-7915.13354 Diamond Proposal Number(s): [9948] Open Access Show Abstract ▼ Abstract: One of the major challenges in chemical synthesis is the selective oxyfunctionalization of non‐activated C‐H bonds, which can be enabled by biocatalysis using cytochrome P450 monooxygenases. In this study, we report on the characterization of the versatile CYP109Q5 from Chondromyces apiculatus DSM436, which is able to functionalize a wide range of substrates (terpenes, steroids and drugs), including the ring of β‐ionone in non‐allylic positions. The crystal structure of CYP109Q5 revealed flexibility within the active site pocket that permitted the accommodation of bulky substrates, and enabled a structure‐guided approach to engineering the enzyme. Some variants of CYP109Q5 displayed a switch in selectivity towards the non‐allylic positions of β‐ionone, allowing the simultaneous production of 2‐ and 3‐hydroxy‐β‐ionone, which are chemically challenging to synthesize and are important precursors for carotenoid synthesis. An efficient whole‐cell system finally enabled the production of up to 0.5 g l−1 hydroxylated products of β‐ionone; this system can be applied to product identification in further biotransformations. Overall, CYP109Q5 proved to be highly evolvable and active. The studies in this work demonstrate that, using rational mutagenesis, the highly versatile CYP109Q5 generalist can be progressively evolved to be an industrially valuable specialist for the synthesis of specific products.	Dec 2018

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