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- W1550173166 abstract "Methanol dehydrogenase (MDH) is a key enzyme in the degradation of methane and methanol by methylotrophic bacteria. It is an oligomeric protein with an α2β2 structure (66 and 10 kDa respectively) and pyrroloquinoline quinone (PQQ) as the redox cofactor, non covalently bound to the large α- subunit. The natural electron acceptor for methanol dehydrogenase is a special type of cytochrome c. The MDH / cytochrome cL couple is an interesting model system to study the interaction and stability of proteins. The interaction of the two proteins can be followed either by the kinetics of electron transfer between the two proteins or by changes in the circular dichroism spectrum. A method based on capillary electrophoresis is presented to determine binding constants of proteins, which is suitable to investigate complex formation between mutant proteins which are no longer capable to transfer electrons. Both proteins are remarkably resistant against denaturation by pressure. Cytochrome cL, a small monomeric protein (19 kDa), is stable up to 1200 MPa. MDH retains its native structure and activity up to 500 MPa, accompanied by a reversible red shift of the 4th derivative absorption spectrum. At pressures above 700 MPa a transition to a denatured state occurs, which is not seen in the presence of cytochrome cL. Application of pressure in the presence of 6 M urea leads to an irreversible and stable change in the 4th derivative absorption spectrum and a concomitant loss of most of the enzymatic activity. No evidence supporting subunit dissociation was obtained." @default.
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- W1550173166 date "1996-01-01" @default.
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- W1550173166 title "Pressure effects on the stability and reactivity of methanol dehydrogenase" @default.
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- W1550173166 doi "https://doi.org/10.1016/s0921-0423(06)80038-9" @default.
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