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putidamonooxin

National Institutes of Health

Papers overview

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2000
2000
Using 4-methoxybenzoate monooxygenase from Pseudomonas putida, the substrate deuterium isotope effect on product formation and… 
1989
1989
1. 4-Methoxybenzoate monooxygenase is fairly nonspecific. The enzyme system with putidamonooxin as its oxygen-activating… 
1985
1985
The mononuclear non-haem iron center is the dioxygen-binding site of putidamonooxin which is the dioxygen-activating component of… 
1985
1985
Mononuclear non-heme cofactor iron of putidamonooxin has been investigated in the binary oxidized 'enzyme X substrate' complex… 
1983
1983
Putidamonooxin, a conjugated iron-sulfur protein, functions as the oxygen-activating component within the 4-methoxybenzoate… 
1981
1981
Putidamonooxin, the oxygenase of a 4-methoxybenzoate monooxygenase enzyme system, catalyzes the oxidative O-demethylation of the… 
1981
1981
In the presence of substrates not favourable for hydroxylation, more than 80% of the dioxygen consumed by purified, reconstituted… 
1981
1981
4-Methoxybenzoate monooxygenase isolated from a species of pseudomonas putida can be separated in two components, NADH… 
1978
1978
Gel chromatography indicates that putidamonooxin has a molecular weight of about 126,000. On the other hand, the amino acid…