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Current Physical Chemistry


ISSN (Print): 1877-9468
ISSN (Online): 1877-9476

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

Author(s): Gerard M. Jensen

Volume 3, Issue 1, 2013

Page: [44 - 54] Pages: 11

DOI: 10.2174/1877946811303010008

open access plus


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.

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