Gene cloning, expression, and reducing property enhancement of nitrous oxide reductase from Alcaligenes denitrificans strain TB

2018 ◽  
Vol 239 ◽  
pp. 43-52 ◽  
Author(s):  
Yu Wang ◽  
Zeyu Wang ◽  
Yankai Duo ◽  
Xiaoping Wang ◽  
Jianmeng Chen ◽  
...  
Keyword(s):  
Nitrous Oxide ◽  
Gene Cloning ◽  
Nitrous Oxide Reductase ◽  
Alcaligenes Denitrificans

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

scholarly journals Conversion of nitrous oxide to nitrogen by cobalt-substituted myoglobin

RSC Advances ◽  
2015 ◽  
Vol 5 (108) ◽  
pp. 89003-89008 ◽  
Author(s):  
Trevor D. Rapson ◽  
Soeren Warneke ◽  
Mustafa M. Musameh ◽  
Helen Dacres ◽  
Ben C. T. Macdonald ◽  
...  
Keyword(s):  
Nitrous Oxide ◽  
Nitrous Oxide Reductase

Turning myoglobin into a nitrous oxide reductase.

scholarly journals Biochemical characterization of the purple form of Marinobacter hydrocarbonoclasticus nitrous oxide reductase

2012 ◽  
Vol 367 (1593) ◽  
pp. 1204-1212 ◽  
Author(s):  
Simone Dell'Acqua ◽  
Sofia R. Pauleta ◽  
José J. G. Moura ◽  
Isabel Moura
Keyword(s):  
Nitrous Oxide ◽  
Redox State ◽  
Biochemical Characterization ◽  
Specific Activity ◽  
Active Species ◽  
Nitrous Oxide Reductase ◽  
Strictly Anaerobic ◽  
Prolonged Incubation ◽  
Redox Active ◽  
Marinobacter Hydrocarbonoclasticus

Nitrous oxide reductase (N 2 OR) catalyses the final step of the denitrification pathway—the reduction of nitrous oxide to nitrogen. The catalytic centre (CuZ) is a unique tetranuclear copper centre bridged by inorganic sulphur in a tetrahedron arrangement that can have different oxidation states. Previously, Marinobacter hydrocarbonoclasticus N 2 OR was isolated with the CuZ centre as CuZ*, in the [1Cu 2+ : 3Cu + ] redox state, which is redox inert and requires prolonged incubation under reductive conditions to be activated. In this work, we report, for the first time, the isolation of N 2 OR from M. hydrocarbonoclasticus in the ‘purple’ form, in which the CuZ centre is in the oxidized [2Cu 2+ : 2Cu + ] redox state and is redox active. This form of the enzyme was isolated in the presence of oxygen from a microaerobic culture in the presence of nitrate and also from a strictly anaerobic culture. The purple form of the enzyme was biochemically characterized and was shown to be a redox active species, although it is still catalytically non-competent, as its specific activity is lower than that of the activated fully reduced enzyme and comparable with that of the enzyme with the CuZ centre in either the [1Cu 2+ : 3Cu + ] redox state or in the redox inactive CuZ* state.

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