Electron delocalization in trinuclear iron-sulfur clusters from Desulfovibrio gigas
نویسندگان
چکیده
منابع مشابه
Redox properties of the iron-sulfur clusters in activated Fe-hydrogenase from Desulfovibrio vulgaris (Hildenborough).
The periplasmic Fe-hydrogenase from Desulfovibrio vulgaris (Hildenborough) contains three iron-sulfur prosthetic groups: two putative electron transferring [4Fe-4S] ferredoxin-like cubanes (two F-clusters), and one putative Fe/S supercluster redox catalyst (one H-cluster). Combined elemental analysis by proton-induced X-ray emission, inductively coupled plasma mass spectrometry, instrumental ne...
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Iron-sulfur ([Fe-S]) clusters, which are among the most ubiquitous and versatile metal centers in biology, require complex machinery for assembly in vivo1,2. Key components of this machinery reside in the mitochondria, where [Fe-S] clusters are assembled on scaffold proteins for eventual transfer to target proteins. Little is understood, however, regarding the assembly and insertion of [FeS] cl...
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Recent Mössbauer and EPR studies of two ferredoxins and of aconitase have given evidence for a three-iron cluster, probably of a [3Fe-3S] type. The studies of the oxidized EPR-active centers have shown that the three iron sites are characterized by significantly different magnetic hyperfine coupling constants. For the ferredoxin from Azotobacter vinelandii, for instance, we have observed A1 = -...
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ژورنال
عنوان ژورنال: Chemical Physics
سال: 1989
ISSN: 0301-0104
DOI: 10.1016/0301-0104(89)80114-4