Unprecedented Oxidative Addition of the P4S3 Cage Molecule with Phosphorus-Phosphorus Bond Cleavage; Synthesis and Molecular Structure of [Ir(?-P4S3)(PPh3)Cl(CO)]2

1983 ◽  
Vol 22 (10) ◽  
pp. 790-791 ◽  
Author(s):  
Carlo A. Ghilardi ◽  
Stefano Midollini ◽  
Annabella Orlandini
Keyword(s):  
Molecular Structure ◽  
Bond Cleavage ◽  
Oxidative Addition ◽  
Cage Molecule

scholarly journals Competitive Te-Te and C-Te bond cleavage in the oxidative addition of diaryl and dialkyl ditellurides to Pt(0) centers

2017 ◽  
Vol 836-837 ◽  
pp. 17-25 ◽  
Author(s):  
Minna M. Karjalainen ◽  
Torben Wiegand ◽  
J. Mikko Rautiainen ◽  
Andreas Wagner ◽  
Helmar Görls ◽  
...  
Keyword(s):  
Bond Cleavage ◽  
Oxidative Addition

scholarly journals Controlling Non-Native B12 Reactivity and Catalysis in the Transcription Factor CarH

2021 ◽  
Author(s):  
Xinhang Yang ◽  
Benjamin H. R. Gerroll ◽  
Yuhua Jiang ◽  
Amardeep Kumar ◽  
Yasmine S. Zubi ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Vitamin B12 ◽  
Transcription Regulation ◽  
Bond Cleavage ◽  
Oxidative Addition ◽  
Mechanistic Studies ◽  
Organic Transformations ◽  
Carbon Bond ◽  
Wide Range ◽  
Hydride Elimination

Vitamin B12 derivatives catalyze a wide range of organic transformations, but B12-dependent enzymes are underutilized in biocatalysis relative to other metalloenzymes. In this study, we engineered a variant of the transcription factor CarH, called CarH*, that catalyzes styrene C-H alkylation with improved yield and selectivity relative to B12 itself. While the native function of CarH involves transcription regulation via AdoCbl Co(III)-carbon bond cleavage and β-hydride elimination to generate 4’,5’-didehydroadenosine, CarH*-catalyzed styrene alkylation proceeds via non-native oxidative addition and olefin addition coupled with a native-like β-hydride elimination. Mechanistic studies on this reaction echo findings from earlier studies on AdoCbl homolysis under strong cage conditions to suggest that CarH* can enable non-native radical chemistry with improved selectivity relative to B12 itself. These findings lay the groundwork for the development of B12-dependent enzymes as catalysts for a wide range of non-native transformations.

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