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Effect of solvent viscosity on the activation barrier of hydrogen tunneling in the lipoxygenase reaction

https://doi.org/10.1016/j.abb.2023.109740

Guevara, Luis; Gouge, Melissa; Ohler, Amanda; Hill, S. Gage; Patel, Soham; Offenbacher, Adam R. (October 2023, Archives of Biochemistry and Biophysics)

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Electrochemical and Structural Study of the Buried Tryptophan in Azurin: Effects of Hydration and Polarity on the Redox Potential of W48

https://doi.org/10.1021/acs.jpcb.2c06677

Tyson, Kristin; Tangtartharakul, Chanin B.; Zeug, Matthias; Findling, Nathan; Haddy, Alice; Hvastkovs, Eli; Choe, Jun-yong; Kim, Judy E.; Offenbacher, Adam R. (December 2022, The Journal of Physical Chemistry B)
Thermodynamic and biophysical study of fatty acid effector binding to soybean lipoxygenase: implications for allostery driven by helix α2 dynamics

https://doi.org/10.1002/1873-3468.14275

Roberts, Daniella E.; Benton, Amy M.; Fabian‐Bayola, Claire; Spuches, Anne M.; Offenbacher, Adam R. (January 2022, FEBS Letters)

Previous comparative kinetic isotope effects have inferred an allosteric site for fatty acids and their derivatives that modulates substrate selectivity in 15‐lipoxygenases. Hydrogen–deuterium exchange also previously revealed regionally defined enhanced protein flexibility, centred at helix α2 – a gate to the substrate entrance. Direct evidence for allosteric binding and a complete understanding of its mechanism remains elusive. In this study, we examine the binding thermodynamics of the fatty acid mimic, oleyl sulfate (OS), with the monomeric model plant 15‐LOX, soybean lipoxygenase (SLO), using isothermal titration calorimetry. Dynamic light scattering and differential scanning calorimetry rule out OS‐induced oligomerization or structural changes. These data provide evidence that the fatty acid allosteric regulation of SLO is controlled by the dynamics of helix α2.
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Mutagenesis, Hydrogen–Deuterium Exchange, and Molecular Docking Investigations Establish the Dimeric Interface of Human Platelet-Type 12-Lipoxygenase

https://doi.org/10.1021/acs.biochem.1c00053

Tsai, Wan-Chen; Aleem, Ansari Mukhtar; Whittington, Chris; Cortopassi, Wilian A.; Kalyanaraman, Chakrapani; Baroz, Angel; Iavarone, Anthony T.; Skrzypczak-Jankun, Ewa; Jacobson, Matthew P.; Offenbacher, Adam R.; et al (March 2021, Biochemistry)

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Synthesis of redox-active fluorinated 5-hydroxytryptophans as molecular reporters for biological electron transfer

https://doi.org/10.1039/d1cc00187f

Ohler, Amanda; Long, Hanna; Ohgo, Kei; Tyson, Kristin; Murray, David; Davis, Amanda; Whittington, Chris; Hvastkovs, Eli G.; Duffy, Liam; Haddy, Alice; et al (January 2021, Chemical Communications)
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Fluorinated 5-hydroxytryptophans (F n -5HOWs) were synthesized in gram scale quantities and incorporated into a β-hairpin peptide and the protein azurin. The redox-active F n -5HOWs exhibit unique radical spectroscopic signatures that expand the function of 5HOW as probes for biological electron transfer.
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