scholarly journals Oxidation of a [Cu2S] complex by N2O and CO2: insights into a role of tetranuclearity in the CuZ site of nitrous oxide reductase

2018 ◽  
Vol 54 (9) ◽  
pp. 1097-1100 ◽  
Author(s):  
Sharareh Bagherzadeh ◽  
Neal P. Mankad
Keyword(s):  
Nitrous Oxide ◽  
Oxidative Stability ◽  
Nitrous Oxide Reductase

N2O reactivity of a [Cu2S] complex implies that tetranuclearity imparts oxidative stability to the CuZ site in nitrous oxide reductase.

scholarly journals Functional assembly of nitrous oxide reductase provides insights into copper site maturation

2019 ◽  
Vol 116 (26) ◽  
pp. 12822-12827 ◽  
Author(s):  
Lin Zhang ◽  
Anja Wüst ◽  
Benedikt Prasser ◽  
Christoph Müller ◽  
Oliver Einsle
Keyword(s):  
Nitrous Oxide ◽  
Nitrous Oxide Reductase ◽  
Heterologous Production ◽  
Heterologous Host ◽  
Metal Centers ◽  
E Coli ◽  
Source Organism ◽  
Copper Site ◽  
Biosynthetic Machinery

The multicopper enzyme nitrous oxide reductase reduces the greenhouse gas N2O to uncritical N2as the final step of bacterial denitrification. Its two metal centers require an elaborate assembly machinery that so far has precluded heterologous production as a prerequisite for bioremediatory applications in agriculture and wastewater treatment. Here, we report on the production of active holoenzyme inEscherichia coliusing a two-plasmid system to produce the entire biosynthetic machinery as well as the structural gene for the enzyme. Using this recombinant system to probe the role of individual maturation factors, we find that the ABC transporter NosFY and the accessory NosD protein are essential for the formation of the [4Cu:2S] site CuZ, but not the electron transfer site CuA. Depending on source organism, the heterologous hostE. colican, in some cases, compensate for the lack of the Cu chaperone NosL, while in others this protein is strictly required, underlining the case for designing a recombinant system to be entirely self-contained.

Theoretically exploring the key role of the Lys412 residue in the conversion of N2O to N2by nitrous oxide reductase from Achromobacter cycloclastes

2015 ◽  
Vol 39 (10) ◽  
pp. 8093-8099 ◽  
Author(s):  
Hujun Xie ◽  
Chengcheng Liu ◽  
Xuelin Chen ◽  
Qunfang Lei ◽  
Wenjun Fang ◽  
...  
Keyword(s):  
Nitrous Oxide ◽  
Nitrous Oxide Reductase ◽  
Achromobacter Cycloclastes ◽  
Back Donation

The active CuZcluster of NOR provides strong back-donation to coordinated N2O and activates the O atom of the N2O group facilitating H-bonding and protonationviathe Lys412 residue.

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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