title: Insights into properties and energetics of iron-sulfur proteins from simple clusters to nitrogenase.
abstract: Some of the principal physical features of iron-sulfur clusters in proteins are analyzed, including metal-ligand covalency, spin polarization, spin coupling, valence delocalization, valence interchange and small reorganization energies, with emphasis on recent spectroscopic and theoretical work. The current state of structural, spectroscopic, and computational knowledge for the iron-sulfur clusters in the nitrogenase iron and iron-molybdenum proteins is examined by comparison and contrast to 'simpler' ironclusters. The differing interactions of the nitrogenase iron and iron-molybdenum clusters compared with those of other iron-sulfur clusters with the protein and solvent environment are also explored.
authors.affiliation: Department of Molecular Biology, TPC15, The Scripps Research Institute, La Jolla, California 92037, USA. lou@scripps.edu
authors.forename: Louis
authors.initials: L
authors.lastname: Noodleman
authors.forename: Timothy
authors.initials: T
authors.lastname: Lovell
authors.forename: Tiqing
authors.initials: T
authors.lastname: Liu
authors.forename: Fahmi
authors.initials: F
authors.lastname: Himo
authors.forename: Rhonda A
authors.initials: RA
authors.lastname: Torres
mesh_terms: D004583:Electrons; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008958:Models, Molecular; D009591:Nitrogenase / Q000737:chemistry*; D010084:Oxidation-Reduction
chemical_list: D007506:Iron-Sulfur Proteins; D009591:Nitrogenase