RT Journal Article
T1 Visualizing the protons in a metalloenzyme electron proton transfer pathway
A1 Kwon, Hanna
A1 Basran, Jaswir
A1 Devos, Juliette
A1 Suardíaz Delrío, Reynier
A1 Van der Kamp, Marc
A1 Mulholland, Adrián
A1 Schrader, Tobias
A1 Ostermann, Andreas
A1 Blakeley, Matthew
A1 Moody, Peter
A1 Raven, Emma
AB In redox metalloenzymes, the process of electron transfer often involves the concerted movement of a proton. These processes are referred to as proton-coupled electron transfer, and they underpin a wide variety of biological processes, including respiration, energy conversion, photosynthesis, and metalloenzyme catalysis. The mechanisms of proton delivery are incompletely understood, in part due to an absence of information on exact proton locations and hydrogen bonding structures in a bona fide metalloenzyme proton pathway. Here, we present a 2.1-Å neutron crystal structure of the complex formed between a redox metalloenzyme (ascorbate peroxidase) and its reducing substrate (ascorbate). In the neutron structure of the complex, the protonation states of the electron/proton donor (ascorbate) and all of the residues involved in the electron/proton transfer pathway are directly observed. This information sheds light on possible proton movements during heme-catalyzed oxygen activation, as well as on ascorbate oxidation.</jats:p>
PB United States National Academy of Sciences
SN 0027-8424
YR 2020
FD 2020
LK https://hdl.handle.net/20.500.14352/92544
UL https://hdl.handle.net/20.500.14352/92544
LA eng
NO Kwon, Hanna, et al. «Visualizing the Protons in a Metalloenzyme Electron Proton Transfer Pathway». Proceedings of the National Academy of Sciences, vol. 117, n.o 12, marzo de 2020, pp. 6484-90. https://doi.org/10.1073/pnas.1918936117.
NO Biotechnology and Biological Sciences Research Council (Reino Unido)
NO Engineering and Physical Sciences Research Council (Reino Unido)
DS Docta Complutense
RD 10 abr 2025