Asset Details
Do you wish to reserve the book?
The role of Tyr34 in proton coupled electron transfer and product inhibition of manganese superoxide dismutase
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
The role of Tyr34 in proton coupled electron transfer and product inhibition of manganese superoxide dismutase
Do you wish to request the book?
The role of Tyr34 in proton coupled electron transfer and product inhibition of manganese superoxide dismutase
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
The role of Tyr34 in proton coupled electron transfer and product inhibition of manganese superoxide dismutase
2025
Overview
Human manganese superoxide dismutase (MnSOD) plays a crucial role in controlling levels of reactive oxygen species (ROS) by converting superoxide (
O
2
∙
−
) to molecular oxygen (O
2
) and hydrogen peroxide (H
2
O
2
) with proton-coupled electron transfers (PCETs). A key catalytic residue, Tyr34, determines the activity of human MnSOD and also becomes post-translationally inactivated by nitration in various diseases associated with mitochondrial dysfunction. Tyr34 has an unusual pK
a
due to its proximity to the Mn metal and undergoes cyclic deprotonation and protonation events to promote the electron transfers of MnSOD. Neutron diffraction, X-ray spectroscopy, and quantum chemistry calculations in oxidized, reduced and product inhibited enzymatic states shed light on the role of Tyr34 in MnSOD catalysis. The data identify the contributions of Tyr34 in MnSOD activity that support mitochondrial function and give a thorough characterization of how a single tyrosine modulates PCET catalysis. Product inhibition occurs by an associative displacement mechanism.
The activity of human manganese superoxide dismutase (MnSOD) is determined by the state of a key catalytic residue, Tyr34, which was reported to undergo cyclic deprotonation and protonation events to promote the electron transfers of MnSOD. Here, the authors performed neutron diffraction, X-ray spectroscopy, and quantum chemistry calculations of Tyr34Phe MnSOD in oxidized, reduced and product inhibited enzymatic states, to elucidate the role of Tyr34 in MnSOD catalysis.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ Enzymes
/ Humanities and Social Sciences
/ Humans
/ Hydrogen Peroxide - metabolism
/ Neutrons
/ Oxygen
/ Protons
/ Reactive Oxygen Species - metabolism
/ Residues
/ Science
/ Superoxide Dismutase - antagonists & inhibitors
/ Superoxide Dismutase - chemistry
/ Superoxide Dismutase - genetics
/ Superoxide Dismutase - metabolism
/ Tyrosine
