The Influence of pH on Long-Range Electron Transfer and Proton-Coupled Electron Transfer in Ruthenium-Modified Azurin.

ABSTRACT: Long-range electron transfer (ET) is an essential component of all biological systems. Reactions of metalloproteins are important in this context. Recent work on protein "charge ladders" has revealed how the redox state of embedded metal ions can influence the ionization of amino acid residues at protein surface sites. Inspired by these observations, we carried out a variable pH investigation of intramolecular ET reactions in a ruthenium-modified protein system built on azurin from Pseudomonas aeruginosa. We also generate a Pourbaix diagram that describes the variable pH redox behavior of a Ru model complex, Ru(2,2'-bipyridyl)₂(imidazole)₂(PF₆)₂. The intramolecular ET rate constants for the oxidation of azurin-Cu⁺ by flash-quenc

SUBMITTER: Ghazi N 

PROVIDER: S-EPMC11821252 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature