Abstract
The purification of the hydroxylase component of a 3 component methane monooxygenase from the type II methanotroph Methylosinus trichosporium OB3b is reported. The enzyme (240 kDa) has an (αβγ)2 subunit structure as observed for hydroxylases isolated from other Type I and Type II methanotrophs, but it exhibits a 5 to 10 fold higher specific activity and is isolated in 2 to 10 fold higher yield. EPR and Mössbauer spectra of the hydroxylase show that it contains a coupled iron center containing an even number of iron atoms. The spectra are similar to those of proteins known to contain oxo-bridged binuclear iron centers. The presence of such a center is unprecedented in a monooxygenase and suggests that a novel mechanism is utilized.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 165-170 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 154 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jul 15 1988 |
Bibliographical note
Funding Information:ACKNOWLEDGEMENTS-This work was supported by NIGMS Grant 24689 and by a grant from the NSF sponsored Center for Biological Process Technology of the University of Minnesota. The authors wish to thank Dr. Eckard Miinck and Ms. Kristine K. Surerus for the measurement of the Mdssbauer spectra and Dr. Richard S. Hanson for many useful discussions. We gratefully acknowledge the technical assistance of Mr. Jay Dege and Mr. Wayne Froland.