Optimization of solubilization and purification procedures for the hydroxylase component of membrane-bound methane monooxygenase from Methylococcus capsulatus strain M.
The hydroxylase component of membrane-bound (particulate) methane monooxygenase (pMMO) from Methylococcus capsulatus strain M was isolated and purified to homogeneity. The pMMO molecule comprises three subunits of molecular masses 47, 26, and 23 kD and contains three copper atoms and one iron atom. In solution the protein exists as a stable oligomer of 660 kD with possible subunit composition (alpha beta gamma)6. Mass spectroscopy shows high homology of the purified protein with methane monooxygenase from Methylococcus capsulatus strain Bath. Pilot screening of crystallization conditions has been carried out.
Vasil'ev
V I
VI
Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, 119071, Russia.
Tikhonova
T V
TV
Gvozdev
R I
RI
Tukhvatullin
I A
IA
Popov
V O
VO
D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification*; D020134:Catalytic Domain; D003300:Copper / Q000737:chemistry; D006867:Hydrolases / Q000737:chemistry / Q000302:isolation & purification*; D007501:Iron / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry / Q000302:isolation & purification*; D020619:Methylococcus capsulatus / Q000201:enzymology*; D010105:Oxygenases / Q000737:chemistry / Q000302:isolation & purification*
D001426:Bacterial Proteins; D008565:Membrane Proteins; D003300:Copper; D007501:Iron; D010105:Oxygenases; C021555:methane monooxygenase; D006867:Hydrolases