Insights into properties and energetics of iron-sulfur proteins from simple clusters to nitrogenase.
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.
Noodleman
Louis
L
Department of Molecular Biology, TPC15, The Scripps Research Institute, La Jolla, California 92037, USA. lou@scripps.edu
Lovell
Timothy
T
Liu
Tiqing
T
Himo
Fahmi
F
Torres
Rhonda A
RA
D004583:Electrons; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008958:Models, Molecular; D009591:Nitrogenase / Q000737:chemistry*; D010084:Oxidation-Reduction
D007506:Iron-Sulfur Proteins; D009591:Nitrogenase