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2016 ; 55
(46
): 6363-6374
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O(2) Activation by Non-Heme Iron Enzymes
#MMPMID27792301
Solomon EI
; Goudarzi S
; Sutherlin KD
Biochemistry
2016[Nov]; 55
(46
): 6363-6374
PMID27792301
show ga
The non-heme Fe enzymes are ubiquitous in nature and perform a wide range of
functions involving O(2) activation. These had been difficult to study relative
to heme enzymes; however, spectroscopic methods that provide significant insight
into the correlation of structure with function have now been developed. This
Current Topics article summarizes both the molecular mechanism these enzymes use
to control O(2) activation in the presence of cosubstrates and the oxygen
intermediates these reactions generate. Three types of O(2) activation are
observed. First, non-heme reactivity is shown to be different from heme chemistry
where a low-spin Fe(III)-OOH non-heme intermediate directly reacts with
substrate. Also, two subclasses of non-heme Fe enzymes generate high-spin
Fe(IV)?O intermediates that provide both ? and ? frontier molecular orbitals that
can control selectivity. Finally, for several subclasses of non-heme Fe enzymes,
binding of the substrate to the Fe(II) site leads to the one-electron reductive
activation of O(2) to an Fe(III)-superoxide capable of H atom abstraction and
electrophilic attack.
|Catalytic Domain
[MESH]
|Circular Dichroism/methods
[MESH]
|Dioxygenases/*chemistry/metabolism
[MESH]
|Enzymes/*chemistry/metabolism
[MESH]
|Hydrogen Bonding
[MESH]
|Kinetics
[MESH]
|Models, Chemical
[MESH]
|Models, Molecular
[MESH]
|Nonheme Iron Proteins/*chemistry/metabolism
[MESH]
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