The role of Tyr34 in proton-coupled electron transfer of human manganese superoxide dismutase
Azadmanesh, J.; Slobodnik, K.; Struble, L. R.; Cone, E. A.; Dasgupta, M.; Lutz, W. E.; Kumar, S.; Natarajan, A.; Coates, L.; Weiss, K. L.; Myles, D.; Kroll, T.; Borgstahl, G. E.
Show abstract
Human manganese superoxide dismutase (MnSOD) plays a crucial role in controlling levels of reactive oxygen species (ROS) by converting superoxide (O2*-) to molecular oxygen (O2) and hydrogen peroxide (H2O2) with proton-coupled electron transfers (PCETs). The reactivity of human MnSOD is determined by the state of a key catalytic residue, Tyr34, that becomes post-translationally inactivated by nitration in various diseases associated with mitochondrial dysfunction. We previously reported that Tyr34 has an unusual pKa due to its proximity to the Mn metal and undergoes cyclic deprotonation and protonation events to promote the electron transfers of MnSOD. To shed light on the role of Tyr34 MnSOD catalysis, we performed neutron diffraction, X-ray spectroscopy, and quantum chemistry calculations of Tyr34Phe MnSOD in various enzymatic states. The data identifies the contributions of Tyr34 in MnSOD activity that support mitochondrial function and presents a thorough characterization of how a single tyrosine modulates PCET catalysis.
Matching journals
The top 5 journals account for 50% of the predicted probability mass.
Similar papers in this journal
Similar papers in this journal
- Revealing the atomic and electronic mechanism of human manganese superoxide dismutase product inhibition 100%
- Direct detection of coupled proton and electron transfers in human manganese superoxide dismutase 98%
- Flavoproteins as native and genetically encoded spin probes for in cell ESR spectroscopy 96%
Similar papers in this journal
Similar papers in this journal
Similar papers in this journal
- Selenocyanate Derived Se-Incorporation into the Nitrogenase Fe Protein Cluster 96%
- Conformational dynamics and asymmetry in multimodal inhibition of membrane-bound pyrophosphatases 96%
- Mechanism of stepwise electron transfer in six-transmembrane epithelial antigen of the prostate (STEAP) 1 and 2 94%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.