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SOR is a non-heme thiolate-ligated metalloenzyme, consisting of a ferrous center ligated by four histidines and a cysteinate residue. It is responsible for superoxide detoxification in anaerobic and microaerophilic organisms by reducing superoxide to hydrogen peroxide. A novel biomimetic model of the active site of SOR, [Fe(II)cyclam-PrS]+ is described. This complex reacts with superoxide under protic conditions at cryogenic temperatures to form the intermediate [Fe(III)cyclam-PrS(OOH)]+. This is a rare example of a high-spin Fe(III)-OOH species, and is the first reported example of a…mehr

Produktbeschreibung
SOR is a non-heme thiolate-ligated metalloenzyme, consisting of a ferrous center ligated by four histidines and a cysteinate residue. It is responsible for superoxide detoxification in anaerobic and microaerophilic organisms by reducing superoxide to hydrogen peroxide. A novel biomimetic model of the active site of SOR, [Fe(II)cyclam-PrS]+ is described. This complex reacts with superoxide under protic conditions at cryogenic temperatures to form the intermediate [Fe(III)cyclam-PrS(OOH)]+. This is a rare example of a high-spin Fe(III)-OOH species, and is the first reported example of a high-spin non-heme Fe(III)-OOH containing a trans thiolate. Using a synthetic approach to achieve biomimicry, new insight into the natural role of thiolates in metalloenzymes is described.
Autorenporträt
Kitagawa, Terutaka,§Terutaka Terence Kitagawa was born on August 18, 1976 in Fremont, California. He earned his B.S. in Chemistry from UCLA in June 2000. He then worked under Julie Kovacs at the University of Washington to study synthetic modeling of non-heme metalloenzymes. In June 2007, he earned a Ph.D in Chemistry from the University of Washington.