A [3Fe-3(μ-S)](3+) cluster is reported in which each ferric center has a distorted trigonal pyramidal geometry, with an S = 1/2 ground state for the cluster and unusually anisotropic hyperfine coupling constants as determined by variable temperature magnetometry and Mössbauer spectroscopy.
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A [3Fe-3S](3+) cluster with exclusively μ-sulfide donors.
Chem Commun (Camb)
January 2016
Department of Chemistry, Center for Catalysis, University of Florida, Gainesville, FL 32611-7200, USA.
A [3Fe-3(μ-S)](3+) cluster is reported in which each ferric center has a distorted trigonal pyramidal geometry, with an S = 1/2 ground state for the cluster and unusually anisotropic hyperfine coupling constants as determined by variable temperature magnetometry and Mössbauer spectroscopy.
View Article and Find Full Text PDF[4Fe-4S]-cluster-depleted Azotobacter vinelandii ferredoxin I: a new 3Fe iron-sulfur protein.
Proc Natl Acad Sci U S A
September 1985
Fe(CN)6(-3) oxidation of the aerobically isolated 7Fe Azotobacter vinelandii ferredoxin I, (7Fe)FdI, is a degradative reaction. Destruction of the [4Fe-4S] cluster occurs first, followed by destruction of the [3Fe-3S] cluster. At a Fe(CN)6(-3)/(7Fe)FdI concentration ratio of 20, the product is a mixture of apoprotein and protein containing only a [3Fe-3S] cluster, (3Fe)FdI.
View Article and Find Full Text PDFThe destructive oxidation of aerobically isolated 7Fe Azotobacter vinelandii ferredoxin I [(7Fe)FdI] by Fe(CN)3-6 is examined using low-temperature magnetic circular dichroism (MCD) and EPR. The results demonstrate that oxidation of the [3Fe-3S] cluster occurs only after essentially complete destruction of the [4Fe-4S] cluster. It is therefore feasible by controlled Fe(CN)3-6 oxidation to obtain a partially metallated form of FdI, (3Fe)FdI, containing only a [3Fe-3S] cluster.
View Article and Find Full Text PDFIron-sulfur cluster in aconitase. Crystallographic evidence for a three-iron center.
J Biol Chem
February 1985
Native x-ray diffraction data from single crystals of inactive aconitase from pig heart (Mr 80,000) have been collected on oscillation films to 2.7 A. Analysis shows that significant measurements of the anomalous scattering signal from the Fe-S cluster in the enzyme are available in the film data.
View Article and Find Full Text PDFSpectroscopic studies of ferricyanide oxidation of Azotobacter vinelandii ferredoxin I.
Proc Natl Acad Sci U S A
April 1984
The Fe(CN)3-(6) oxidation of the crystallographically characterized [[3Fe-3S], [4Fe-4S]] ferredoxin I of Azotobacter vinelandii has been studied using absorption, circular dichroism, magnetic circular dichroism, and EPR spectroscopies. A paramagnetic intermediate is observed en route to Fe-S cluster-free apoprotein, possessing an anisotropic g approximately equal to 2 EPR signal, surviving to temperatures greater than 77 K. This species is shown to result from 3-electron oxidation of the [4Fe-4S] cluster, without modification of the [3Fe-3S] cluster.
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