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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography	CYP153A71 from Alcanivorax dieselolei: oxidation beyond monoterminal hydroxylation of n-alkanes Cheri Louise Jacobs , Rodolpho Do Aido-Machado , Carmien Tolmie , Martha Sophia Smit , Diederik Johannes Opperman Catalysts 12 DOI: 10.3390/catal12101213 Diamond Proposal Number(s): [20303] Open Access Show Abstract ▼ Abstract: Selective oxyfunctionalization of non-activated C–H bonds remains a major challenge in synthetic chemistry. The biocatalytic hydroxylation of non-activated C–H bonds by cytochrome P450 monooxygenases (CYPs), however, offers catalysis with high regio- and stereoselectivity using molecular oxygen. CYP153s are a class of CYPs known for their selective terminal hydroxylation of n-alkanes and microorganisms, such as the bacterium Alcanivorax dieselolei, have evolved extensive enzymatic pathways for the oxyfunctionalization of various lengths of n-alkanes, including a CYP153 to yield medium-chain 1-alkanols. In this study, we report the characterization of the terminal alkane hydroxylase from A. dieselolei (CYP153A71) for the oxyfunctionalization of medium-chain n-alkanes in comparison to the well-known CYP153A6 and CYP153A13. Although the expected 1-alkanols are produced, CYP153A71 readily converts the 1-alkanols to the corresponding aldehydes, fatty acids, as well as α,ω-diols. CYP153A71 is also shown to readily hydroxylate medium-chain fatty acids. The X-ray crystal structure of CYP153A71 bound to octanoic acid is solved, yielding an insight into not only the regioselectivity, but also the binding orientation of the substrate, which can be used in future studies to evolve CYP153A71 for improved oxidations beyond terminal n-alkane hydroxylation.	Oct 2022
I04-1-Macromolecular Crystallography (fixed wavelength)	Natural variation in the ‘control loop’ of BVMOAFL210 and its influence on regioselectivity and sulfoxidation Carmien Tolmie , Rodolpho Do Aido-Machado , Felix Martin Ferroni , Martha Sophia Smit , Diederik Johannes Opperman Catalysts 10 DOI: 10.3390/catal10030339 Diamond Proposal Number(s): [18938] Open Access Show Abstract ▼ Abstract: Baeyer-Villiger monooxygenases (BVMOs) are flavin-dependent enzymes that primarily convert ketones to esters, but can also catalyze heteroatom oxidation. Several structural studies have highlighted the importance of the ‘control loop’ in BVMOs, which adopts different conformations during catalysis. Central to the ‘control loop’ is a conserved tryptophan that has been implicated in NADP(H) binding. BVMOAFL210 from Aspergillus flavus, however, contains a threonine in the equivalent position. Here, we report the structure of BVMOAFL210 in complex with NADP+ in both the ‘open’ and ‘closed’ conformations. In neither conformation does Thr513 contact the NADP+. Although mutagenesis of Thr513 did not significantly alter the substrate scope, changes in peroxyflavin stability and reaction rates were observed. Mutation of this position also brought about changes in the regio- and enantioselectivity of the enzyme. Moreover, lower rates of overoxidation during sulfoxidation of thioanisole were also observed.	Mar 2020

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