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Super-exchange and Exchange-Enhanced Reactivity in Fe_(4)S_(4)-Mediated Activation of SAM by Radical SAM Enzymes
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作者 Jian-qiang Feng Bin-ju Wang 《Chinese Journal of Chemical Physics》 SCIE CAS CSCD 2021年第5期532-540,I0002,共10页
[4Fe-4S]-dependent radical S-adenosylmethionine(SAM)proteins are a superfamily of oxidoreductases that can catalyze a series of challenging transformations using the common 5-d Ado radical intermediate.Although the st... [4Fe-4S]-dependent radical S-adenosylmethionine(SAM)proteins are a superfamily of oxidoreductases that can catalyze a series of challenging transformations using the common 5-d Ado radical intermediate.Although the structures and functions of radical SAM enzymes have been extensively studied,the electronic state-dependent reactions of the[4Fe-4S]clusters in these enzymes are still elusive.Herein we performed QM/MM calculations to elucidate the electronic state-dependent reactivity of the[4Fe-4S]cluster in pyruvate-formate lyase activating enzyme.Our calculations show that the electronic statedependent SAM activation by the[4Fe-4S]clusters in radical SAM enzyme is determined by both the super-exchange and exchange-enhanced reactivities.The super-exchange coupling in the[4Fe-4S]cluster favors the antiferromagnetic coupling between two neighbouring pairs,which results in theα-electron rather than theβ-electron donation from the[4Fe-4S]^(1+)cluster toward the SAM activation.Meanwhile,in the most favorable electronic state for the reductive cleavage of S-C5′,Fe4 would donate itsα-electron to gain the maximum exchange interactions in the Fe4-block.Such super-exchange and exchange-enhanced reactivity could be the general principles for reactivities of[4Fe-4S]cluster in RS enzymes. 展开更多
关键词 QM/MM Iron-sulfur protein Electron transfer Super-exchange exchange-enhanced reactivity Radical SAM enzyme
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