F430 model chemistry. Mechanistic investigation of the reduction, coupling, and dehydrohalogenation of alkyl halides by the nickel(I) octaethylisobacteriochlorin anion

Lahiri, Goutam Kumar; Schussel, Leonard J.; Stolzenberg, Alan M.

doi:10.1021/ic00050a016

Cited by 59 publications

(45 citation statements)

References 5 publications

(5 reference statements)

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“…The stability of [Ni I (oeibc)] Ϫ is greatest in polar solvents. With weak acids such as water, alcohols, and thiols it affords H 2 with an apparent stoichiometry of 2:1 Ni I :H 2 [43].…”

Section: Methodsmentioning

confidence: 99%

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Synthetic Models for the Active Sites of Nickel‐Containing Enzymes

Vlugt

Meyer

2007

Nickel and Its Surprising Impact in Nature

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“…The stability of [Ni I (oeibc)] Ϫ is greatest in polar solvents. With weak acids such as water, alcohols, and thiols it affords H 2 with an apparent stoichiometry of 2:1 Ni I :H 2 [43].…”

Section: Methodsmentioning

confidence: 99%

“…The reactions of [Ni I (oeibc)] Ϫ with alkyl and aryl halides give organic products that result from reduction or dehydrohalogenation [43,44]; alkene formation is favored by polar solvents, and isomerization of alkenes occurs during reaction. This implies the intermediacy of Ni-H and Ni-R species in the reactions.…”

Section: Methodsmentioning

confidence: 99%

Synthetic Models for the Active Sites of Nickel‐Containing Enzymes

Vlugt

Meyer

2007

Nickel and Its Surprising Impact in Nature

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“…-. 53 Other Ni I isobacteriochlorin (iBC) complexes, which contain the fused cyclohexanone ring of F 430 , can be analogously prepared. 44 [Ni(OEiBC)] -has not only spectroscopic relevance to MCR red1 , but also exhibits reactivity that has some similarities to that of MCR.…”

Section: Background On Nickel(i) and On Methyl Com Reductase (Mcr)mentioning

confidence: 99%

Overview of ligand versus metal centered redox reactions in tetraaza macrocyclic complexes of nickel with a focus on electron paramagnetic resonance studies

Telser

2010

J. Braz. Chem. Soc.

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Complexos de cobre(II) (3d 9 , S = 1/2) são estáveis e amplamente investigados por espectroscopia de ressonância paramagnética eletrônica (EPR). Já o isoeletrônico níquel(I) é muito menos comum e muito menos estudado. No entanto, níquel(I) tem interesse biológico, uma vez que o sítio ativo da metil coenzima M redutase (MCR) , S = 1/2) complexes are stable and widely investigated by electron paramagnetic resonance (EPR) spectroscopy. In contrast, isoelectronic nickel(I) is much less common and much less investigated. Nickel(I), however, is of biological interest as the active site of methyl coenzyme M reductase (MCR) contains a tetraaza macrocyclic ligand, F 430 , which coordinates Ni I in its active form, MCR red1 . As result, the redox behavior and spectroscopy of tetraaza macrocyclic complexes of nickel is of importance in biomimetic chemistry. Such efforts are complicated by the difficulty in generating Ni I from their stable, Ni II , precursors. Reduction of Ni II macrocyclic complexes can afford Ni I in certain cases, but in many other cases can lead instead to reduction of the macrocycle to generate an organic radical anion. Previous studies on the formation of tetraaza macrocyclic complexes of Ni I are discussed in terms of the competition between metal-centered and ligandcentered reduction. EPR results are particularly important in making the distinction between these two reduction processes, as formation of Ni I gives characteristic EPR spectra similar to those for Cu II , while ligand-centered reduction gives narrow EPR spectra at g = 2.00, typical of organic radicals. Even if metal-centered reduction occurs, the geometry of the resulting Ni I macrocyclic complex is highly variable and, as a result, the EPR spectral appearance is highly variable. In this case, the comparison is between the extremes of spectra typical for tetragonally distorted complexes (dx2-y2 1 ground state, which includes tetragonally distorted octahedral, square pyramidal and square planar geometries) and those for trigonal bipyramidal complexes (dz2 1 ground state). Previous work on Cu II was related to the situation for Ni I . The different types of EPR spectra for such systems are specifically discussed using previously unpublished examples of several tetraaza macrocyclic complexes of nickel, including F 430 and MCR itself.

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“…Coenzyme F 430 can be used to catalyze the reductive dehalogenation of chlorinated or brominated hydrocarbons [79][80][81]. Several F 430 model compounds have been shown to have the same property [82][83][84][85][86]. The reaction of alkylhalides with Ni(I)F 430 can mechanistically explain why 2-bromoethanesulfonate and 3-bromopropanesulfonate are suicide inhibitors of active methyl-coenzyme M reductase [ The UV-visible spectrum of Ni(III)F 430 shows an absorption maximum at 360 nm (ε ϭ 16 mM Ϫ1 cm Ϫ1 ; MeCN) and the EPR spectrum consists of a strongly anisotropic signal of the axial type (g ⊥ ϭ 2.211 and g ʈ ϭ 2.020) with barely resolved fi ne structure on the g ʈ line and no resolved structure on the g ⊥ part.…”

Section: Properties Of Ni(ii)f 430 and Nonplanaritymentioning

confidence: 99%

Methyl‐Coenzyme M Reductase and its Nickel Corphin Coenzyme F ₄₃₀ in Methanogenic Archaea

Jaun

Thauer

2007

Nickel and Its Surprising Impact in Nature

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F430 model chemistry. Mechanistic investigation of the reduction, coupling, and dehydrohalogenation of alkyl halides by the nickel(I) octaethylisobacteriochlorin anion

Cited by 59 publications

References 5 publications

Synthetic Models for the Active Sites of Nickel‐Containing Enzymes

Synthetic Models for the Active Sites of Nickel‐Containing Enzymes

Overview of ligand versus metal centered redox reactions in tetraaza macrocyclic complexes of nickel with a focus on electron paramagnetic resonance studies

Methyl‐Coenzyme M Reductase and its Nickel Corphin Coenzyme F ₄₃₀ in Methanogenic Archaea

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F430 model chemistry. Mechanistic investigation of the reduction, coupling, and dehydrohalogenation of alkyl halides by the nickel(I) octaethylisobacteriochlorin anion

Cited by 59 publications

References 5 publications

Synthetic Models for the Active Sites of Nickel‐Containing Enzymes

Synthetic Models for the Active Sites of Nickel‐Containing Enzymes

Overview of ligand versus metal centered redox reactions in tetraaza macrocyclic complexes of nickel with a focus on electron paramagnetic resonance studies

Methyl‐Coenzyme M Reductase and its Nickel Corphin Coenzyme F 430 in Methanogenic Archaea

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Methyl‐Coenzyme M Reductase and its Nickel Corphin Coenzyme F ₄₃₀ in Methanogenic Archaea