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/1 Asp structural motif analogous to alpha-ketoglutarate dependent dioxygenases are presented. The calculations show that these oxidants are very efficient and able to hydroxylate strong C-H bonds, whereby the hydrogen abstraction barriers correlate linearly with the strength of the C-H bond of the substrate that is broken. These trends have been rationalized using a valence bond (VB) curve-crossing diagram, which explains the correlation using electron transfer mechanisms in the hydrogen abstraction processes. We also rationalized the subsequent reaction step for radical rebound and show that the barrier is proportional to the electron affinity of the iron(III)-hydroxo intermediate complex. It is shown that nonheme iron(IV)-hydroxo complexes have a larger electron affinity than heme iron(IV)-hydroxo complexes and therefore also experience larger radical rebound barriers, which may have implications for product distributions and rearrangement reactions. Thus, detailed comparisons between heme and nonheme iron(IV)-oxo oxidants reveal the fundamental differences in monoxygenation capabilities of these important classes of oxidants in biosystems and synthetic analogues for the first time and enable us to make predictions of experimental processes.