@article{chen_bowden_2013, title={Electrochemical characterization of dehaloperoxidase adsorbates on COOH/OH mixed self-assembled monolayers}, volume={703}, ISSN={["1873-2569"]}, DOI={10.1016/j.jelechem.2013.05.023}, abstractNote={Electrochemical characterization of Amphitrite ornata dehaloperoxidase, a monomeric hemoglobin, adsorbed on COOH/OH-terminated alkanethiolate mixed self-assembled monolayers (SAMs) is reported. Adsorption was achieved by simple electrode exposure to low ionic strength protein solution at pH 6.0, and cyclic voltammetry (CV) was employed to measure surface concentration, electron transfer rate, and formal potential under anaerobic conditions. Surface concentration values determined by CV were found to be inversely proportional to scan rate, a behavior that is different than that observed for electron transfer proteins such as cytochrome c. We attribute this behavior to a dynamic heterogeneous adsorbate layer that permits some fraction of the molecules to undergo reorientation during a CV scan. A model was proposed that classifies adsorbates among three populations with respect to their most stable orientations, namely, electroactive adsorbates, latent electroinactive adsorbates capable of undergoing reorientation to electroactive states, and electroinactive adsorbates. Electrochemical results and the proposed model are discussed in terms of the tertiary structure and surface properties of dehaloperoxidase and are compared to the docking and electron transfer reactions of the myoglobin/cytochrome b5 system. Examination of the effects of ionic strength and mixed SAM composition provide support for the proposed model.}, journal={JOURNAL OF ELECTROANALYTICAL CHEMISTRY}, author={Chen, Thomas K. and Bowden, Edmond F.}, year={2013}, month={Aug}, pages={23–28} }
 @article{d'antonio_chen_turner_santiago-capeles_bowden_2013, title={Voltammetry of dehaloperoxidase on self-assembled monolayers: Reversible adsorptive immobilization of a globin}, volume={26}, ISSN={1388-2481}, url={http://dx.doi.org/10.1016/j.elecom.2012.10.011}, DOI={10.1016/j.elecom.2012.10.011}, abstractNote={Abstract Dehaloperoxidase (DHP), a monomeric hemoglobin, was adsorptively immobilized under low ionic strength conditions on binary self-assembled monolayers composed of OH- and COOH-terminated alkylthiols. Voltammetry of its Fe(III)/Fe(II) reactions revealed adsorbed DHP to be electroactive and native under both anaerobic and aerobic conditions. The chemically reversible nature of the adsorptive immobilization was established from voltammetric desorption/re-adsorption experiments. Cyclic voltammetric determination of electroactive surface concentration uncovered an unusual inverse scan rate dependence that was rationalized by means of Hoffman's dynamic docking electron transfer model [Z.-X. Liang et al., J. Am. Chem. Soc. 126 (2004) 2785]. This result represents the first evidence for dynamic docking control of protein electron transfer in an electrochemical setting.}, journal={Electrochemistry Communications}, publisher={Elsevier BV}, author={D'Antonio, Edward L. and Chen, Thomas K. and Turner, Abigail H. and Santiago-Capeles, Lisandra and Bowden, Edmond F.}, year={2013}, month={Jan}, pages={67–70} }