Calculating standard reduction potentials of [4Fe–4S] proteins. Issue 7 (1st November 2012)

• Record Type: Journal Article
• Authors: Perrin, Bradley Scott; Niu, Shuqiang; Ichiye, Toshiko
• Is Part Of: Journal of computational chemistry. Volume 34:Issue 7(2013)
• Page Start: 576
• Page End: 582
• Publication Date: 2012-11-01
• Subjects: Chemistry -- Data processing -- Periodicals; 542.85
• DOI: 10.1002/jcc.23169
• Languages: English
• ISSNs: 0192-8651

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>The oxidation–reduction potentials of electron transfer proteins determine the driving forces for their electron transfer reactions. Although the type of redox site determines the intrinsic energy required to add or remove an electron, the electrostatic interaction energy between the redox site and its surrounding environment can greatly shift the redox potentials. Here, a method for calculating the reduction potential <italic>versus</italic> the standard hydrogen electrode, <italic>E</italic>°, of a metalloprotein using a combination of density functional theory and continuum electrostatics is presented. This work focuses on the methodology for the continuum electrostatics calculations, including various factors that may affect the accuracy. The calculations are demonstrated using crystal structures of six homologous HiPIPs, which give <italic>E</italic>° that are in excellent agreement with experimental results. © 2012 Wiley Periodicals, Inc.</p> </abstract>