Spin NO Complexes with Non-Heme Iron Proteins

Low-Spin NO Complexes with Non-Heme Iron Proteins 

A remaining question is whether the new d iron-nitrosyl center might involve a rearrangement to include the sulfurs of the zinc center. The extremely tight binding of zinc to the second metal site in Fur suggests not, but accounting quantita- 

The x-ray structure of Fur from Pseudomonas aeruginosa, solved recently [64], is the first structure of a Fur protein. In this organism the protein has only one sulf-hydryl, and it lacks the domain with the high-affinity zinc site of the E. coli homolog. Still, it was found to have two metal sites, one (O4/N2) octahedral site for iron and one tetrahedral (O2/N2) site occupied by zinc. All the metal-binding amino acids are conserved in the P. aeruginosa and E. coli homologs, so an unidentified 

Gaffney B J, Silverstone HJ. 1993. Simulation of the EMR spectra of high-spin iron in proteins. In EMR of paramagnetic molecules, pp. 1-57. Ed LJ Berliner, J Reuben. Biological magnetic resonance, Vol. 13. New York London Plenum Press. 

Abu-Omar MM, Loaiza A, Hontzeas N. 2005. Reaction mechanisms of mononuclear non-heme iron oxygenases. Chem Rev 105(6) 2227-2252. 

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