Iron-Sulfur Clusters in Proteins: Mutagenesis Studies and Theoretical Predictions of the Control of Redox Potential - A Review

Author(s): Gerard M. Jensen

Journal Name: Current Physical Chemistry

Volume 3 , Issue 1 , 2013

Become EABM
Become Reviewer
Call for Editor


Redox proteins and enzymes containing iron-sulfur clusters continue to emerge as key elements of cellular metabolism. Proteins and clusters of enormous complexity continue to succumb to experimental definition, such as nitrogenase and hydrogenase enzymes. Simpler systems, including iron-sulfur clusters of the general formula FexSy(SCys) z, have long been subject to fundamental research, including the theoretical modeling of cluster redox potential in variable protein environments. In this review, we explore results obtained on these systems, which are only relatively simple. If the efforts reviewed continue to flourish, they can form the foundation for methods and basic physical principles relevant to the most complex systems.

Keywords: Iron-sulfur, Ferredoxin, Rubredoxin, Redox, Protein dielectric, Effective dielectric, nitrogenase, atmospheric nitrogen, anionic mass, cysteine ligands.

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2013
Published on: 20 January, 2013
Page: [44 - 54]
Pages: 11
DOI: 10.2174/1877946811303010008

Article Metrics

PDF: 17