Visualizing the protons in a metalloenzyme electron proton transfer pathway

Hanna Kwon, Jaswir Basran, Juliette M. Devos, Reynier Suardiaz Del Rio, Marc W Van Der Kamp, Adrian J Mulholland, Tobias E. Schrader, Andreas Ostermann, Matthew P. Blakeley, Peter C. E. Moody, Emma Raven

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Abstract

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 new light on possible proton movements during heme-catalysed oxygen activation, as well as on ascorbate oxidation.

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Keywords

  • heme
  • proton transfer
  • neutron
  • abscorbate
  • peroxidase

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