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Understanding the Mechanism of Short-Range Electron Transfer Using an Immobilized Cupredoxin

Lookup NU author(s): Sachiko Yanagisawa, Dr Isabelle Salard-Arnaud, Dorota Kostrz, Professor Christopher Dennison

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Abstract

The hydrophobic patch of, azurin (AZ) from Pseudomonas aeruginosa is an important recognition surface for electron transfer (ET) reactions. The influence of changing the size of this region, by mutating the C-terminal copper binding loop, on the ET reactivity of AZ adsorbed on gold electrodes modified with alkanethiol self-assembled monolayers (SAMs) has been studied. The distance-dependence of ET kinetics measured by cyclic voltammetry using SAMs of variable chain length, demonstrates that the activation barrier for short-range ET is dominated by the dynamics of molecular rearrangements accompanying ET at the AZ-SAM interface. These include internal electric field dependent low amplitude protein motions and the reorganization of interfacial water molecules, but not protein reorientation. Interfacial molecular dynamics also control the kinetics of short-range ET for electrostatically and covalently immobilized cytochrome c. This mechanism therefore may be utilized for short-distance ET irrespective of the type of metal center, the surface electrostatic potential, and the nature of the protein- SAM interaction.


Publication metadata

Author(s): Monari S, Battistuzzi G, Bortolotti CA, Yanagisawa S, Sato K, Li C, Salard I, Kostrz D, Borsari M, Ranieri A, Dennison C, Sola M

Publication type: Article

Publication status: Published

Journal: Journal of the American Chemical Society

Year: 2012

Volume: 134

Issue: 29

Pages: 11848-11851

Print publication date: 12/07/2012

ISSN (print): 0002-7863

ISSN (electronic): 1520-5126

Publisher: American Chemical Society

URL: http://dx.doi.org/10.1021/ja303425b

DOI: 10.1021/ja303425b


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