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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

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

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 + FADox 14.3 66 Monomer–Dimer
14.0 74 Monomer–Dimer
10.8 273 Oligomer
7.9 Polymer
StyA1 + FADred 13.8 81 Dimer
StyA2B 12.9 116 Dimer
9.4 Oligomer
8.3 Polymer
StyA2B + FADox 13.0 112 Dimer
9.4 Oligomer
8.3 Polymer
StyA2B + FADred 13.1 107 Dimer
StyA 15.2 46 Monomer
13.7 84 Dimer
11.5 205 Tetramer
StyA + FADox 15.1 48 Monomer
13.5 91 Dimer
StyA + FADred 15.0 50 Monomer
  1. 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.