Potassium barium hexanitrocuprate(II) at 295 K

Takagi, S.; Joesten, Melvin D.; Lenhert, P. G.

doi:10.1107/s0567740875003329

Cited by 20 publications

(3 citation statements)

References 3 publications

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“…The short distance in the latter species and in L i -Pr 3 Cu(NO 2 ) presumably reflects an increased M−NO 2 bond order arising from π-back-donation from filled metal orbitals to the lowest energy nitrite π* orbital ( vide infra ). Significantly longer Cu−N nitrite bonds (≥2.0 Å) have been reported for various salts of the Cu(II) species Cu(NO 2 ) n x - ( n = 5, x = 3; n = 6, x = 4), although disorders involving possible static and/or dynamic Jahn-Teller distortions complicate comparisons to crystallographic data obtained for many of these compounds . Finally, as is typical for transition metal nitro complexes, in L i -Pr 3 Cu(NO 2 ), the nitrite O−N−O angle [116.0(2)°] and N−O distances [1.253(5) and 1.238(5) Å] differ only slightly from those of the free nitrite ion [114.9(5)° and 1.240(3) Å, respectively], the approximate equivalence of the distances being consistent with the expected lack of bond alternation.…”

Section: Resultsmentioning

confidence: 99%

Synthetic Modeling of Nitrite Binding and Activation by Reduced Copper Proteins. Characterization of Copper(I)−Nitrite Complexes That Evolve Nitric Oxide

et al. 1996

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In an effort to provide precedence for postulated intermediates in copper-protein-mediated nitrite reduction, a series of novel complexes containing the Cu I -NO 2 -unit, including monocopper(I), dicopper(I,I), and mixed valence dicopper(I,II) and copper(I)-zinc(II) species, were prepared, fully characterized, and subjected to reactivity studies designed to probe their ability to produce nitric oxide. Treatment of solutions of [LCu(CH 3 CN)]PF 6 (L ) L i-Pr 3 , 1,4,7-triisopropyl-1,4,7-triazacyclononane, or L Bn 3 , 1,4,7-tribenzyl-1,4,7-triazacyclononane) in MeOH with excess NaNO 2 yielded the novel dicopper(I,I) complexes [(LCu) 2 (µ-NO 2 )]PF 6 . The complex with L ) L i-Pr 3 was cleaved by PPh 3 to afford [L i-Pr 3 Cu(PPh 3 )]PF 6 and L i-Pr 3 Cu(NO 2 ), a structural model for the substrate adduct of copper nitrite reductase. Oxidation of the dicopper(I,I) compound (L ) L i-Pr 3 ) with (Cp 2 Fe)(PF 6 ) in CH 2 Cl 2 yielded the deep red, mixed valent, dicopper(I,II) species [(L i-Pr 3 Cu) 2 (µ-NO 2 )](PF 6 ) 2 , which was structurally characterized as its [B(3,5-(CF 3 ) 2 C 6 H 3 ) 4 ] -salt (crystal data: triclinic space group P1 h, a ) 13.439(8) Å, b ) 13.777(5) Å, c ) 14.471(8) Å, R ) 108.22(4)°, β ) 92.08(5)°, γ ) 90.08(4)°, Z ) 1, T ) 177 K, R ) 0.074, and R w ) 0.070). A diamagnetic heterodinuclear Cu I Zn II analog, [L i-Pr 3 Cu(µ-NO 2 )ZnL i-Pr 3 ](O 3 SCF 3 ) 2 , was assembled by mixing L i-Pr 3 Cu(NO 2 ), Zn(O 3 -SCF 3 ) 2 , and L i-Pr 3 and was shown to adopt a structure similar to that of its Cu I Cu II relative (crystal data: monoclinic space group P2 1 /c, a ) 10.8752(1) Å, b ) 15.6121(3) Å, c ) 25.8020(5) Å, β ) 90.094(1)°, Z ) 4, R1 ) 0.0472, and wR2 ) 0.1082). Both compounds exhibit an intense electronic absorption feature that was assigned as a Cu I f NO 2 -MLCT transition on the basis of resonance Raman spectroscopic results.

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Section: Resultsmentioning

confidence: 99%

Synthetic Modeling of Nitrite Binding and Activation by Reduced Copper Proteins. Characterization of Copper(I)−Nitrite Complexes That Evolve Nitric Oxide

et al. 1996

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“…A key step in this mechanism is the formation of a reduced enzyme-substrate complex, E-Cu I -NO 2 -. Numerous copper(II)-nitrite complexes exist, [187][188][189][190][191][192][193][194][195][196][197][198][199][200][201][202] while none of these have demonstrated the ability to mimic the enzymatic reduction of nitrite to nitric oxide and water. Copper(II)-nitrite systems actually form rather stable complexes that do not support nitric oxide formation.…”

Section: Synthetic Copper Complexes: Models For the Type 2 Cu Of Nirmentioning

confidence: 99%

Nitric Oxide in Biological Denitrification: Fe/Cu Metalloenzyme and Metal Complex NO_x Redox Chemistry

et al. 2002

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Ian M. Wasser was born in 1973 in the suburbs of Detroit, Michigan and graduated from Detroit Country Day School. He received a B. S. Chemistry degree in chemistry from the University of Michigan in 1995, where he conducted undergraduate research under the direction of Professor James E. Penner-Hahn. This was then followed in 1998 by an M. S. degree in chemistry from the University of California at Berkeley, where he studied organometallic chemistry and X-ray crystallography with Professor Peter Vollhardt. He is currently a doctoral candidate, working toward his Ph.D. in bioinorganic chemistry under the direction of Professor Kenneth D. Karlin at Johns Hopkins University, where his research focuses on the interactions of synthetic iron and copper complexes with nitric oxide.

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“…The unique case reported by Rommelius (1692) differs from ours in that the side showing excessive sweating varied with the posture, occurring only on the side that was uppermost when the patient lay in bed. This was presumably an exaggeration of a phenomenon that is now known to occur in normal subjects (Takagi and Kobayasi, 1956;Ferres, 1958).…”

Section: Discussionmentioning

confidence: 93%

Unilateral Hyperhidrosis of the Trunk

Champion

Herxheimer

1960

Journal of Internal Medicine

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Potassium barium hexanitrocuprate(II) at 295 K

Abstract: KzBaCu(NO2)6, orthorhombic, Fmmm, a= 11.219 (2), b= 10.

Cited by 20 publications

References 3 publications

Synthetic Modeling of Nitrite Binding and Activation by Reduced Copper Proteins. Characterization of Copper(I)−Nitrite Complexes That Evolve Nitric Oxide

Synthetic Modeling of Nitrite Binding and Activation by Reduced Copper Proteins. Characterization of Copper(I)−Nitrite Complexes That Evolve Nitric Oxide

Nitric Oxide in Biological Denitrification: Fe/Cu Metalloenzyme and Metal Complex NO_x Redox Chemistry

Unilateral Hyperhidrosis of the Trunk

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Potassium barium hexanitrocuprate(II) at 295 K

Abstract: KzBaCu(NO2)6, orthorhombic, Fmmm, a= 11.219 (2), b= 10.

Cited by 20 publications

References 3 publications

Synthetic Modeling of Nitrite Binding and Activation by Reduced Copper Proteins. Characterization of Copper(I)−Nitrite Complexes That Evolve Nitric Oxide

Synthetic Modeling of Nitrite Binding and Activation by Reduced Copper Proteins. Characterization of Copper(I)−Nitrite Complexes That Evolve Nitric Oxide

Nitric Oxide in Biological Denitrification: Fe/Cu Metalloenzyme and Metal Complex NOx Redox Chemistry

Unilateral Hyperhidrosis of the Trunk

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Nitric Oxide in Biological Denitrification: Fe/Cu Metalloenzyme and Metal Complex NO_x Redox Chemistry