putidamonooxin

 
National Institutes of Health

Topic mentions per year

Topic mentions per year

1978-2006
012319782006

Papers overview

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2006
2006
Putidamonooxin (PMO) the oxygenase of a 4-methoxybenzoate monooxygenase catalyzes in presence of the NADH-PMO oxidoreductase… (More)
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2000
2000
Using 4-methoxybenzoate monooxygenase from Pseudomonas putida, the substrate deuterium isotope effect on product formation and… (More)
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1989
1989
1. 4-Methoxybenzoate monooxygenase is fairly nonspecific. The enzyme system with putidamonooxin as its oxygen-activating… (More)
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1985
1985
The mononuclear non-haem iron center is the dioxygen-binding site of putidamonooxin which is the dioxygen-activating component of… (More)
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1985
1985
Mononuclear non-heme cofactor iron of putidamonooxin has been investigated in the binary oxidized 'enzyme X substrate' complex… (More)
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1985
1985
The investigations presented in this paper were performed on two enzyme systems from Pseudomonas putida: (a) 4-methoxybenzoate… (More)
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1981
1981
In the presence of substrates not favourable for hydroxylation, more than 80% of the dioxygen consumed by purified, reconstituted… (More)
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1981
1981
Putidamonooxin, the oxygenase of a 4-methoxybenzoate monooxygenase enzyme system, catalyzes the oxidative O-demethylation of the… (More)
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1978
1978
Gel chromatography indicates that putidamonooxin has a molecular weight of about 126,000. On the other hand, the amino acid… (More)
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