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[23] Monophenol monooxygenase from Neurospora crassa
Methods in Enzymology, 1987openaire +3 more sources
Biotechnology and Bioengineering, 2015
ABSTRACTTyrosinase is a binuclear copper‐containing metalloprotein that leads the fast and regio‐selective o‐hydroxylation of monophenols to o‐diphenols. However, the subsequent second oxidation to produce o‐quinones, i.e., melanin precursors, from the o‐diphenols has restricted its use to the production of functional o‐diphenol derivatives. Herein, we
Sang-Hyuk, Lee +3 more
openaire +2 more sources
ABSTRACTTyrosinase is a binuclear copper‐containing metalloprotein that leads the fast and regio‐selective o‐hydroxylation of monophenols to o‐diphenols. However, the subsequent second oxidation to produce o‐quinones, i.e., melanin precursors, from the o‐diphenols has restricted its use to the production of functional o‐diphenol derivatives. Herein, we
Sang-Hyuk, Lee +3 more
openaire +2 more sources
Ukrains'kyi biokhimichnyi zhurnal (1999 ), 2001
The intracellular localization and some properties of monophenol monooxygenase (MPMO) from fresh tea leaves have been studied. It has been demonstrated that MPMO activity is located in cytosole and chloroplasts. These two forms have different properties. Molecular weights of cytosole and chloroplasts MPMO are 41 and 28 kD respectively. The chloroplasts
N T, Omiadze +3 more
openaire +1 more source
The intracellular localization and some properties of monophenol monooxygenase (MPMO) from fresh tea leaves have been studied. It has been demonstrated that MPMO activity is located in cytosole and chloroplasts. These two forms have different properties. Molecular weights of cytosole and chloroplasts MPMO are 41 and 28 kD respectively. The chloroplasts
N T, Omiadze +3 more
openaire +1 more source
Mechanistic Studies on the Hydroxylation of Methane by Methane Monooxygenase
Chemical Reviews, 2003Mu-Hyun Baik +2 more
exaly