Metal−Metal Cooperativity Effects in Promoting C−H Bond Cleavage of a Methyl Group by an Adjacent Metal Center

1999 ◽  
Vol 121 (15) ◽  
pp. 3666-3683 ◽  
Author(s):  
Jeffrey R. Torkelson ◽  
Frederick H. Antwi-Nsiah ◽  
Robert McDonald ◽  
Martin Cowie ◽  
Justin G. Pruis ◽  
...  
Keyword(s):  
Bond Cleavage ◽  
Metal Center ◽  
Methyl Group ◽  
Metal Metal ◽  
Cooperativity Effects

Metal-Metal Cooperative Bond Activation by Heterobimetallic Alkyl, Aryl, and Acetylide PtII/CuI Complexes

2020 ◽  
Author(s):  
Shubham Deolka ◽  
Orestes Rivada Wheelaghan ◽  
Sandra Aristizábal ◽  
Robert Fayzullin ◽  
Shrinwantu Pal ◽  
...  
Keyword(s):  
Alkyl Group ◽  
Bond Activation ◽  
Bond Cleavage ◽  
Terminal Alkyne ◽  
Alkyl Aryl ◽  
Metal Metal ◽  
The Stability ◽  
Selective Formation ◽  
Organoplatinum Compounds

We report selective formation of heterobimetallic PtII/CuI complexes that demonstrate how facile bond activation processes can be achieved by altering reactivity of common organoplatinum compounds through their interaction with another metal center. The interaction of the Cu center with Pt center and with a Pt-bound alkyl group increases the stability of PtMe2 towards undesired rollover cyclometalation. The presence of the CuI center also enables facile transmetalation from electron-deficient tetraarylborate [B(ArF)4]- anion and mild C-H bond cleavage of a terminal alkyne, which was not observed in the absence of an electrophilic Cu center. The DFT study indicates that the role of Cu center acts as a binding site for alkyne substrate, while activating its terminal C-H bond.

Ultrafast studies of metal-metal bond cleavage in Fe3(CO)12 in solution

1995 ◽  
Vol 229 (1-2) ◽  
pp. 469-471 ◽  
Author(s):  
N.J. Tro ◽  
J.C. King ◽  
C.B. Harris
Keyword(s):  
Bond Cleavage ◽  
Metal Bond ◽  
Metal Metal

scholarly journals Proteogenomics Reveals Novel Reductive Dehalogenases and Methyltransferases Expressed during Anaerobic Dichloromethane Metabolism

2019 ◽  
Vol 85 (6) ◽  
Author(s):  
Sara Kleindienst ◽  
Karuna Chourey ◽  
Gao Chen ◽  
Robert W. Murdoch ◽  
Steven A. Higgins ◽  
...  
Keyword(s):  
Amino Acid ◽  
Reductive Dechlorination ◽  
Bond Cleavage ◽  
Amino Acid Identity ◽  
Methyl Group ◽  
Acid Identity ◽  
Group Transfer ◽  
Degrading Bacterium ◽  
Chlorine Bond ◽  
Methyl Group Transfer

ABSTRACTDichloromethane (DCM) is susceptible to microbial degradation under anoxic conditions and is metabolized via the Wood-Ljungdahl pathway; however, mechanistic understanding of carbon-chlorine bond cleavage is lacking. The microbial consortium RM contains the DCM degrader “CandidatusDichloromethanomonas elyunquensis” strain RM, which strictly requires DCM as a growth substrate. Proteomic workflows applied to DCM-grown consortium RM biomass revealed a total of 1,705 nonredundant proteins, 521 of which could be assigned to strain RM. In the presence of DCM, strain RM expressed a complete set of Wood-Ljungdahl pathway enzymes, as well as proteins implicated in chemotaxis, motility, sporulation, and vitamin/cofactor synthesis. Four corrinoid-dependent methyltransferases were among the most abundant proteins. Notably, two of three putative reductive dehalogenases (RDases) encoded within strain RM’s genome were also detected in high abundance. Expressed RDase 1 and RDase 2 shared 30% amino acid identity, and RDase 1 was most similar to an RDase ofDehalococcoides mccartyistrain WBC-2 (AOV99960, 52% amino acid identity), while RDase 2 was most similar to an RDase ofDehalobactersp. strain UNSWDHB (EQB22800, 72% amino acid identity). Although the involvement of RDases in anaerobic DCM metabolism has yet to be experimentally verified, the proteome characterization results implicated the possible participation of one or more reductive dechlorination steps and methyl group transfer reactions, leading to a revised proposal for an anaerobic DCM degradation pathway.IMPORTANCENaturally produced and anthropogenically released DCM can reside in anoxic environments, yet little is known about the diversity of organisms, enzymes, and mechanisms involved in carbon-chlorine bond cleavage in the absence of oxygen. A proteogenomic approach identified two RDases and four corrinoid-dependent methyltransferases expressed by the DCM degrader “CandidatusDichloromethanomonas elyunquensis” strain RM, suggesting that reductive dechlorination and methyl group transfer play roles in anaerobic DCM degradation. These findings suggest that the characterized DCM-degrading bacteriumDehalobacterium formicoaceticumand “CandidatusDichloromethanomonas elyunquensis” strain RM utilize distinct strategies for carbon-chlorine bond cleavage, indicating that multiple pathways evolved for anaerobic DCM metabolism. The specific proteins (e.g., RDases and methyltransferases) identified in strain RM may have value as biomarkers for monitoring anaerobic DCM degradation in natural and contaminated environments.

Intermolecular Methyl Group Exchange and Reversible P–Me Bond Cleavage at Cobalt(III) Dimethyl Halide Species

2013 ◽  
Vol 32 (3) ◽  
pp. 798-806 ◽  
Author(s):  
Hongwei Xu ◽  
Paul G. Williard ◽  
Wesley H. Bernskoetter
Keyword(s):  
Bond Cleavage ◽  
Methyl Group

Metal-metal bond cleavage in [Cp(CO)2Fe-Fe(CO)2Cp] under the action of organotellurium(IV)tribromides

2012 ◽  
Vol 38 (3) ◽  
pp. 219-223 ◽  
Author(s):  
Y. V. Torubaev ◽  
A. V. Pavlova ◽  
A. A. Pasynskii
Keyword(s):  
Bond Cleavage ◽  
Metal Bond ◽  
Metal Metal
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