Catalytic and hydrodynamic properties of styrene monooxygenases from Rhodococcus opacus 1CP are modulated by cofactor binding

AMB Express

Table 3 Hydrodynamic properties of StyA oxygenases from R. opacus 1CP as monitored by analytical gel filtration in the absence or presence of (reduced) FAD

StyA oxygenase	Elution volume (mL)^a	Apparent molecular mass (kDa)^a	Hydrodynamic state
StyA1	14.3	66	Monomer–Dimer
	14.0	75	Monomer–Dimer
	11.1	241	Oligomer
	8.2	≫	Polymer
StyA1 + FAD_ox	14.3	66	Monomer–Dimer
	14.0	74	Monomer–Dimer
	10.8	273	Oligomer
	7.9	≫	Polymer
StyA1 + FAD_red	13.8	81	Dimer
StyA2B	12.9	116	Dimer
	9.4	≫	Oligomer
	8.3	≫	Polymer
StyA2B + FAD_ox	13.0	112	Dimer
	9.4	≫	Oligomer
	8.3	≫	Polymer
StyA2B + FAD_red	13.1	107	Dimer
StyA	15.2	46	Monomer
	13.7	84	Dimer
	11.5	205	Tetramer
StyA + FAD_ox	15.1	48	Monomer
StyA + FAD_ox	13.5	91	Dimer
StyA + FAD_red	15.0	50	Monomer

^aSuperdex 200 column, bed volume = 22.0 mL. The mean of apparent molecular mass of repeated runs of protein samples is shown and the calculated standard deviation was between 5 and 10% in all cases.