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10.1021/acs.biochem.6b00635 http://scihub22266oqcxt.onion/10.1021/acs.biochem.6b00635 C5345855!5345855!27792301     free     free     free       Biochemistry 2016 ; 55 (46): 6363-74 Nephropedia Template TP {{tp|p=27792301|t=2016. O2 activation by non-heme iron enzymes |pdf=|usr=}}{{27792301}} gab.com Text O2 activation by non-heme iron enzymes JO: Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=27792301 #FOAvip The non-heme Fe enzymes are ubiquitous in nature and perform a wide range of functions involving O2 activation. These had been difficult to study relative to heme enzymes; however, spectroscopic methods have now been developed that provide significant insight into the correlation of structure with function. This Current Topics article summarizes both the molecular mechanism these enzymes use to control O2 activation in the presence of cosubstrates and the oxygen intermediates these reactions generate. Three types of O2 activation are observed. First, non-heme reactivity is shown to be different from heme chemistry where a low-spin FeIII-OOH non-heme intermediate directly reacts with substrate. Also, two subclasses of non-heme Fe enzymes generate high-spin FeIV=O intermediates that provide both ? and ? frontier molecular orbitals that can control selectivity. Finally, for several subclasses of non-heme Fe enzymes, substrate binding to the FeII site leads to the one electron reductive activation of O2 to an FeIII-superoxide capable of H-atom abstraction and electrophilic attack. Twit Text FOAVip O2 activation by non-heme iron enzymes ????Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=27792301 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27792301 #FOAvip English Wikipedia <ref>{{Cite pmid|27792301}}</ref> O2 activation by non-heme iron enzymes #MMPMID27792301 Solomon EI; Goudarzi S; Sutherlin KD Biochemistry 2016[Nov]; 55 (46): 6363-74 PMID27792301show ga The non-heme Fe enzymes are ubiquitous in nature and perform a wide range of functions involving O2 activation. These had been difficult to study relative to heme enzymes; however, spectroscopic methods have now been developed that provide significant insight into the correlation of structure with function. This Current Topics article summarizes both the molecular mechanism these enzymes use to control O2 activation in the presence of cosubstrates and the oxygen intermediates these reactions generate. Three types of O2 activation are observed. First, non-heme reactivity is shown to be different from heme chemistry where a low-spin FeIII-OOH non-heme intermediate directly reacts with substrate. Also, two subclasses of non-heme Fe enzymes generate high-spin FeIV=O intermediates that provide both ? and ? frontier molecular orbitals that can control selectivity. Finally, for several subclasses of non-heme Fe enzymes, substrate binding to the FeII site leads to the one electron reductive activation of O2 to an FeIII-superoxide capable of H-atom abstraction and electrophilic attack. äO2 activation by non-heme iron enzymes (epmc).pdf DeepDyve Pubget Overpricing