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putidamonooxin

National Institutes of Health

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Oxygenases

Papers overview

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2005
2005
Kinetics of reduction of putidamonooxin by NADH-putidamonooxin oxidoreductase, sodium dithionite and superoxide radicals.
Putidamonooxin, a conjugated iron-sulfur protein, functions as the oxygen-activating component within the 4-methoxybenzoate… 
2000
2000
Substrate and solvent isotope effects on the fate of the active oxygen species in substrate-modulated reactions of putidamonooxin.
Using 4-methoxybenzoate monooxygenase from Pseudomonas putida, the substrate deuterium isotope effect on product formation and… 
1989
1989
Substrate-modulated reactions of putidamonooxin. The nature of the active oxygen species formed and its reaction mechanism.
1. 4-Methoxybenzoate monooxygenase is fairly nonspecific. The enzyme system with putidamonooxin as its oxygen-activating… 
1985
1985
Protein-protein interactions and antigenic relationships between the components of 4-methoxybenzoate monooxygenase and of benzene 1,2-dioxygenase from Pseudomonas putida.
The investigations presented in this paper were performed on two enzyme systems from Pseudomonas putida: (a) 4-methoxybenzoate… 
1981
1981
Mössbauer studies on the active Fe ... [2Fe-2S] site of putidamonooxin, its electron transport and dioxygen activation mechanism.
Putidamonooxin, the oxygenase of a 4-methoxybenzoate monooxygenase enzyme system, catalyzes the oxidative O-demethylation of the… 
1981
1981
An electron-spin-resonance study on the redox-active centers of the 4-methoxybenzoate monooxygenase from Pseudomonas putida.
4-Methoxybenzoate monooxygenase isolated from a species of pseudomonas putida can be separated in two components, NADH… 
1981
1981
Mössbauer studies on the cofactor of Putidamonooxin (PMO)
Putidamonooxin (PMO) the oxygenase of a 4-methoxybenzoate monooxygenase catalyzes in presence of the NADH-PMO oxidoreductase… 
1980
1980
Mössbauer and kinetic studies on putidamonooxin (PMO)
1980
1980
Dioxygen activation by putidamonooxin – The influence of substrate analogues on the fate of the active oxygen species
1978
1978
Chemical and spectral properties of putidamonooxin, the iron-containing and acid-labile-sulfur-containing monooxygenase of a 4-methoxybenzoate O-demethylase from Pseudomonas putida.
Gel chromatography indicates that putidamonooxin has a molecular weight of about 126,000. On the other hand, the amino acid… 
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