Document Detail


Comparative Reactivity of Ferric-Superoxo and Ferryl-Oxo Species in Heme and non-Heme Complexes.
MedLine Citation:
PMID:  22047171     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Ferryl-oxo species have been recognized as a key oxidant in many heme and non-heme enzymes. Recently, less-characterized ferric-superoxo species have been found or suggested to be another electrophilic oxidant. Reactivity of several vital ferryl-oxo and ferric-superoxo model complexes was examined by DFT calculations. The reactivity is found to correlate well with thermodynamic driving force, and can in-crease with higher electrophilicity of the oxidant. The reactiv-ity of the ferric-superoxo oxidants generally is not "superior" to the ferryl-oxo ones. Compared to the high-spin non-heme ferric-superoxo, the lower reactivity of the low-spin heme ferric-superoxo, seldom utilized in nature, can be attributed to the lower electrophilicity and more pronounced quenching of anti-ferromagnetic coupling between the ferric and the super-oxo part. The present comparison should shed some light on the mechanistic strategies in heme and non-heme enzymes and provide clues to rational design of ferric-superoxo oxidants.
Authors:
Lung Wa Chung; Xin Li; Hajime Hirao; Keiji Morokuma
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-11-2
Journal Detail:
Title:  Journal of the American Chemical Society     Volume:  -     ISSN:  1520-5126     ISO Abbreviation:  -     Publication Date:  2011 Nov 
Date Detail:
Created Date:  2011-11-3     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7503056     Medline TA:  J Am Chem Soc     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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