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Origin of the correlation of the rate constant of substrate hydroxylation by nonheme iron(IV)-oxo complexes with the bond-dissociation energy of the C-H bond of the substrate
, Article Chemistry - A European Journal ; Volume 15, Issue 27 , 2009 , Pages 6651-6662 ; 09476539 (ISSN) ; Bagherzadeh, M ; De Visser, S ; Sharif University of Technology
Wiley-VCH Verlag
2009
Abstract
Mononuclear nonheme iron containing systems are versatile and vital oxidants of substrate hydroxylation reactions in many biosystems, whereby the rate constant of hydroxylation correlates with the strength of the C-H bond that is broken in the process. The thermodynamic reason behind these correlations, however, has never been established. In this work results of a series of density functional theory calculations of substrate hydroxylation by a mononuclear nonheme iron(IV)-oxo oxidant with a 2 His/ 1Asp structural motif analogous to aketoglutarate dependent dioxygenases are presented. The calculations show that these oxidants are very efficient and able to hydroxylate strong C-H bonds,...