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Nature of Labile Sulfur

Models of the Iron Coordination Structure A. Chemical Nature of Labile Sulfur [Pg.26]

An intriguing chemical feature of non-heme iron proteins of the ferredoxin group is the so-called labile sulfur . There is some contradiction in interpretations of the chemical nature of this unusual sulfur . [Pg.26]

and Kazmaier (7) proposed that labile sulfur originates from cysteinyl residues by a p-elimination reaction in the presence of [Pg.26]

Therefore, the hairpin-type linear arrangement of iron atoms bridged with sulfur atoms, proposed independently by Blomstrom et al. (10), Tanaka et al. (64), and Brinzinger et al. (11) is generally favored. [Pg.27]

The third structure of labile sulfur is a persulfide linkage which has been proposed by Massey and his coworkers (39) for dihydroorotate dehydrogenase. This enzyme has 2 atoms of iron, and 2 moles of labile sulfur besides its flavin moiety. They suggested that in catalysis the iron sulfide functions as an iron-sulfur radical, and the iron is not reduced by substrate. [Pg.27]


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