the monomeric form of PHBH, which is not achieved under conventional conditions, is isolated by entrapment in reverse micelles and by addition of DMSO. The PHBH monomer is catalytically more efficient than the PHBH dimer
the monomeric form of PHBH, which is not achieved under conventional conditions, is isolated by entrapment in reverse micelles and by addition of DMSO. The PHBH monomer is catalytically more efficient than the PHBH dimer
structure modeling of the PhhA subunit, the FAD-binding domain, the FAD cofactor, the substrate-binding domain, the thioredoxin domain, and substrate 4-hydroxybenzoate, overview
structure modeling of the PhhA subunit, the FAD-binding domain, the FAD cofactor, the substrate-binding domain, the thioredoxin domain, and substrate 4-hydroxybenzoate, overview
both subunits contain flavin adenine dinucleotide (FAD), which interacts with nicotinamide adenine dinucleotide phosphate (NADPH) and 4-hydroxybenzoate to form a ternary complex that allows the oxygenation of 4-hydroxybenzoate by the reduction of FAD. Each PobA chain in the structure contains 20 beta-strands and 15 alpha-helices, secondary structure analysis, overview
both subunits contain flavin adenine dinucleotide (FAD), which interacts with nicotinamide adenine dinucleotide phosphate (NADPH) and 4-hydroxybenzoate to form a ternary complex that allows the oxygenation of 4-hydroxybenzoate by the reduction of FAD. Each PobA chain in the structure contains 20 beta-strands and 15 alpha-helices, secondary structure analysis, overview
both subunits contain flavin adenine dinucleotide (FAD), which interacts with nicotinamide adenine dinucleotide phosphate (NADPH) and 4-hydroxybenzoate to form a ternary complex that allows the oxygenation of 4-hydroxybenzoate by the reduction of FAD. Each PobA chain in the structure contains 20 beta-strands and 15 alpha-helices, secondary structure analysis, overview