Synthetic models for bis-metallo active sites. A porphyrin capped by a tetrakis(pyridine) ligand system

1978 ◽  
Vol 100 (9) ◽  
pp. 2899-2901 ◽  
Author(s):  
David A. Buckingham ◽  
Maxwell J. Gunter ◽  
Lewis N. Mander
Keyword(s):  
Active Sites ◽  
Pyridine Ligand ◽  
Ligand System ◽  
Synthetic Models

Synthetic models for active sites of reduced blue copper proteins: minimal geometric change between two oxidation states for fast self-exchange rate constants

2004 ◽  
Vol 7 (11) ◽  
pp. 1188-1190 ◽  
Author(s):  
Kiyoshi Fujisawa ◽  
Koyu Fujita ◽  
Tatsuya Takahashi ◽  
Nobumasa Kitajima ◽  
Yoshihiko Moro-oka ◽  
...  
Keyword(s):  
Exchange Rate ◽  
Rate Constants ◽  
Active Sites ◽  
Oxidation States ◽  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Blue Copper ◽  
Synthetic Models

scholarly journals Partial synthetic models of FeMoco with sulfide and carbyne ligands: Effect of interstitial atom in nitrogenase active site

2021 ◽  
Vol 118 (49) ◽  
pp. e2109241118
Author(s):  
Linh N. V. Le ◽  
Gwendolyn A. Bailey ◽  
Anna G. Scott ◽  
Theodor Agapie
Keyword(s):  
Active Sites ◽  
Chemical Properties ◽  
Metal Centers ◽  
Bridging Ligand ◽  
Reduction Potentials ◽  
Protein Active Sites ◽  
Physical And Chemical ◽  
Synthetic Models ◽  
And Chemical Properties

Nitrogen-fixing organisms perform dinitrogen reduction to ammonia at an Fe-M (M = Mo, Fe, or V) cofactor (FeMco) of nitrogenase. FeMco displays eight metal centers bridged by sulfides and a carbide having the MFe7S8C cluster composition. The role of the carbide ligand, a unique motif in protein active sites, remains poorly understood. Toward addressing how the carbon bridge affects the physical and chemical properties of the cluster, we isolated synthetic models of subsite MFe3S3C displaying sulfides and a chelating carbyne ligand. We developed synthetic protocols for structurally related clusters, [Tp*M’Fe3S3X]n−, where M’ = Mo or W, the bridging ligand X = CR, N, NR, S, and Tp* = Tris(3,5-dimethyl-1-pyrazolyl)hydroborate, to study the effects of the identity of the heterometal and the bridging X group on structure and electrochemistry. While the nature of M’ results in minor changes, the chelating, μ3-bridging carbyne has a large impact on reduction potentials, being up to 1 V more reducing compared to nonchelating N and S analogs.

New dicopper(II/II) Complexes with Oxygen and Sulfur Bridges: Synthesis, Characterization and Cyclic Voltammetric Studies

2000 ◽  
Vol 2000 (2) ◽  
pp. 58-59
Author(s):  
Uday Mukhopadhyay ◽  
Debashis Ray
Keyword(s):  
Active Sites ◽  
Cyclic Voltammetric ◽  
Dinuclear Copper ◽  
New Family ◽  
Voltammetric Studies ◽  
Cyclic Voltammetric Studies ◽  
First Time ◽  
Synthetic Models

A new family of acetato oxygen and dithiocarbonato sulfur bridged dinuclear copper(II) complexes with weak imidazolidine bridge support is described for the first time; these complexes are studied for possible synthetic models of dicopper active sites.

scholarly journals Cluster Models of FeMoco with Sulfide and Carbyne Ligands: Effect of Interstitial Atom in Nitrogenase Active Site

2021 ◽  
Author(s):  
Linh Le ◽  
Gwendolyn Bailey ◽  
Anna Scott ◽  
Theodor Agapie
Keyword(s):  
Active Sites ◽  
Interstitial Atom ◽  
Metal Centers ◽  
Bridging Ligand ◽  
Reduction Potentials ◽  
Formal Charge ◽  
Protein Active Sites ◽  
Cluster Composition ◽  
Synthetic Models

<p>Nitrogen-fixing organisms perform dinitrogen reduction to ammonia at an iron-M (M = Mo, Fe, or V) cofactor (FeMco) of nitrogenase. FeMoco displays eight metal centers bridged by sulfides and a carbide having the MoFe<sub>7</sub>S<sub>8</sub>C cluster composition. The role of the carbide ligand, a unique motif in protein active sites, remains poorly understood. Toward addressing its function, we isolated synthetic models of subsite MFe<sub>3</sub>S<sub>3</sub>C displaying sulfides and a carbyne ligand. We developed synthetic protocols for structurally related clusters, [Tp*MFe<sub>3</sub>S<sub>3</sub>X]<sup>n-</sup>, where M = Mo or W, the bridging ligand X = CR, N, NR, S, and Tp* = tris(3,5-dimethyl-1-pyrazolyl)hydroborate, to study the effects of the identity of the heterometal and the bridging X group on structure and electrochemistry. While the nature of M results in minor changes, the μ<sub>3</sub>-bridging ligand X has a large impact on reduction potentials, with differences higher than 1 V, even for the same formal charge, the most reducing clusters being supported by the carbyne ligand. </p>

scholarly journals Stepwise Assembly of Heterobimetallic Complexes: Synthesis, Structure, and Physical Properties

2021 ◽  
Author(s):  
Justin L Lee ◽  
Victoria Frances Oswald ◽  
Saborni Biswas ◽  
Ethan A Hill ◽  
Joseph W Ziller ◽  
...  
Keyword(s):  
Physical Properties ◽  
Structure Function ◽  
Active Sites ◽  
Heterobimetallic Complexes ◽  
Structure Function Relationship ◽  
Function Relationship ◽  
Stepwise Assembly ◽  
Synthetic Models

Bimetallic active sites are ubiquitous in metalloenzymes and has sparked investigations of synthetic models to aid in the establishment of structure-function relationship. We previously reported a series of discrete bimetallic...

scholarly journals Reversible Alkylation at the Pyridine Nitrogen in a α,α‘-Diimine Pyridine Ligand System

2002 ◽  
Vol 21 (17) ◽  
pp. 3678-3678
Author(s):  
Ilia Khorobkov ◽  
Sandro Gambarotta ◽  
Glenn P. A. Yap ◽  
Peter H. M. Budzellar
Keyword(s):  
Pyridine Ligand ◽  
Ligand System ◽  
Pyridine Nitrogen

scholarly journals Cluster Models of FeMoco with Sulfide and Carbyne Ligands: Effect of Interstitial Atom in Nitrogenase Active Site

2021 ◽  
Author(s):  
Linh Le ◽  
Gwendolyn Bailey ◽  
Anna Scott ◽  
Theodor Agapie
Keyword(s):  
Active Sites ◽  
Interstitial Atom ◽  
Metal Centers ◽  
Bridging Ligand ◽  
Reduction Potentials ◽  
Formal Charge ◽  
Protein Active Sites ◽  
Cluster Composition ◽  
Synthetic Models

<p>Nitrogen-fixing organisms perform dinitrogen reduction to ammonia at an iron-M (M = Mo, Fe, or V) cofactor (FeMco) of nitrogenase. FeMoco displays eight metal centers bridged by sulfides and a carbide having the MoFe<sub>7</sub>S<sub>8</sub>C cluster composition. The role of the carbide ligand, a unique motif in protein active sites, remains poorly understood. Toward addressing its function, we isolated synthetic models of subsite MFe<sub>3</sub>S<sub>3</sub>C displaying sulfides and a carbyne ligand. We developed synthetic protocols for structurally related clusters, [Tp*MFe<sub>3</sub>S<sub>3</sub>X]<sup>n-</sup>, where M = Mo or W, the bridging ligand X = CR, N, NR, S, and Tp* = tris(3,5-dimethyl-1-pyrazolyl)hydroborate, to study the effects of the identity of the heterometal and the bridging X group on structure and electrochemistry. While the nature of M results in minor changes, the μ<sub>3</sub>-bridging ligand X has a large impact on reduction potentials, with differences higher than 1 V, even for the same formal charge, the most reducing clusters being supported by the carbyne ligand. </p>

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