Impact of Electronic and Steric Changes of Ligands on the Assembly, Stability, and Redox Activity of Cu4(μ4-S) Model Compounds of the CuZ Active Site of Nitrous Oxide Reductase (N2OR)

2020 ◽  
Vol 59 (9) ◽  
pp. 6496-6507 ◽  
Author(s):  
Suresh C. Rathnayaka ◽  
Chia-Wei Hsu ◽  
Brittany J. Johnson ◽  
Sarah J. Iniguez ◽  
Neal P. Mankad
Keyword(s):  
Nitrous Oxide ◽  
Active Site ◽  
Redox Activity ◽  
Nitrous Oxide Reductase ◽  
Model Compounds ◽  
S Model

scholarly journals The tetranuclear copper active site of nitrous oxide reductase: the CuZ center

2011 ◽  
Vol 16 (2) ◽  
pp. 183-194 ◽  
Author(s):  
Simone Dell’Acqua ◽  
Sofia R. Pauleta ◽  
Isabel Moura ◽  
José J. G. Moura
Keyword(s):  
Nitrous Oxide ◽  
Active Site ◽  
Nitrous Oxide Reductase

scholarly journals A [3Cu:2S] cluster provides insight into the assembly and function of the CuZ site of nitrous oxide reductase

2021 ◽  
Author(s):  
Lin Zhang ◽  
Eckhard Bill ◽  
Peter M. H. Kroneck ◽  
Oliver Einsle
Keyword(s):  
Nitrous Oxide ◽  
Active Site ◽  
Structural Flexibility ◽  
Nitrous Oxide Reductase ◽  
Metal Site ◽  
And Function ◽  
Insight Into

Variants of all seven histidine ligands of the [4Cu:2S] active site of nitrous oxide reductase mostly result in loss of the metal site. However, a H382A variant retains a [3Cu:2S] cluster that hints towards a structural flexibility also present in the intact site.

scholarly journals Assembly, Structure, and Reactivity of Cu4S and Cu3S Models for the Nitrous Oxide Reductase Active Site, CuZ*

2014 ◽  
Vol 53 (19) ◽  
pp. 10611-10619 ◽  
Author(s):  
Brittany J. Johnson ◽  
Sergey V. Lindeman ◽  
Neal P. Mankad
Keyword(s):  
Nitrous Oxide ◽  
Active Site ◽  
Nitrous Oxide Reductase ◽  
Assembly Structure

N2O reduction at a dissymmetric {Cu2S}-containing mixed-valent center

2014 ◽  
Vol 5 (12) ◽  
pp. 4774-4784 ◽  
Author(s):  
Charlène Esmieu ◽  
Maylis Orio ◽  
Stéphane Torelli ◽  
Laurent Le Pape ◽  
Jacques Pécaut ◽  
...  
Keyword(s):  
Nitrous Oxide ◽  
Active Site ◽  
Room Temperature ◽  
Nitrous Oxide Reductase ◽  
N2o Reduction

Through a bio-inspired approach of the active site of the metalloenzyme nitrous oxide reductase, we isolated and characterized a dinuclear mixed-valent dicopper complex capable of N2O reduction at room temperature.

The nature of the copper centres in nitrous oxide reductase (Pseudomonas stutzeri)

1991 ◽  
Vol 43 (2-3) ◽  
pp. 181
Author(s):  
Jacqui A. Farrar ◽  
Andrew J. Thomson ◽  
Myles R. Cheesman ◽  
David M. Dooley ◽  
Walter G. Zumft
Keyword(s):  
Nitrous Oxide ◽  
Pseudomonas Stutzeri ◽  
Nitrous Oxide Reductase
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