Dataset Information

Proton-coupled electron hopping in Ru-modified P. aeruginosa azurin.

ABSTRACT: We constructed two artificial multiple-step electron transfer (hopping) systems based on Pseudomonas aeruginosa azurin where a tyrosine (YOH) is situated between Ru(2,2'-bipyridine)2(imidazole)(histidine) and the native copper site: RuH107YOH109 and RuH124-YOH122. We investigated the rates of Cu(I) oxidation by flash-quench generated Ru(III) over a range of conditions that probed the role of proton-coupled oxidation/reduction of YOH in the reaction. Rates of Cu(I) oxidation were enhanced over single-step electron transfer by factors between 3 and 80, depending on specific scaffold and buffer conditions.

SUBMITTER: Warren JJ

PROVIDER: S-EPMC4775413 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature

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Publications

Proton-coupled electron hopping in Ru-modified P. aeruginosa azurin.

Warren Jeffrey J JJ Shafaat Oliver S OS Winkler Jay R JR Gray Harry B HB

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry 20160120 1

We constructed two artificial multiple-step electron transfer (hopping) systems based on Pseudomonas aeruginosa azurin where a tyrosine (YOH) is situated between Ru(2,2'-bipyridine)2(imidazole)(histidine) and the native copper site: RuH107YOH109 and RuH124-YOH122. We investigated the rates of Cu(I) oxidation by flash-quench generated Ru(III) over a range of conditions that probed the role of proton-coupled oxidation/reduction of YOH in the reaction. Rates of Cu(I) oxidation were enhanced over si ...[more]

PMID: 26790882

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Project description:Designing molecular platforms for controlling proton and electron movement in artificial photosynthetic systems is crucial to efficient catalysis and solar energy conversion. The transfer of both protons and electrons during a reaction is known as proton-coupled electron transfer (PCET) and is used by nature in myriad ways to provide low overpotential pathways for redox reactions and redox leveling, as well as to generate bioenergetic proton currents. Herein, we describe theoretical and electrochemical studies of a series of bioinspired benzimidazole-phenol (BIP) derivatives and a series of dibenzimidazole-phenol (BI2P) analogs with each series bearing the same set of terminal proton-accepting (TPA) groups. The set of TPAs spans more than 6 pK a units. These compounds have been designed to explore the role of the bridging benzimidazole(s) in a one-electron oxidation process coupled to intramolecular proton translocation across either two (the BIP series) or three (the BI2P series) acid/base sites. These molecular constructs feature an electrochemically active phenol connected to the TPA group through a benzimidazole-based bridge, which together with the phenol and TPA group form a covalent framework supporting a Grotthuss-type hydrogen-bonded network. Infrared spectroelectrochemistry demonstrates that upon oxidation of the phenol, protons translocate across this well-defined hydrogen-bonded network to a TPA group. The experimental data show the benzimidazole bridges are non-innocent participants in the PCET process in that the addition of each benzimidazole unit lowers the redox potential of the phenoxyl radical/phenol couple by 60 mV, regardless of the nature of the TPA group. Using a series of hypothetical thermodynamic steps, density functional theory calculations correctly predicted the dependence of the redox potential of the phenoxyl radical/phenol couple on the nature of the final protonated species and provided insight into the thermodynamic role of dibenzimidazole units in the PCET process. This information is crucial for developing molecular "dry proton wires" with these moieties, which can transfer protons via a Grotthuss-type mechanism over long distances without the intervention of water molecules.

Dataset Information

Proton-coupled electron hopping in Ru-modified P. aeruginosa azurin.

Publications

Proton-coupled electron hopping in Ru-modified P. aeruginosa azurin.

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