Abstract:
:The ribonucleotide reductase from the strictly anaerobic methanogen Methanobacterium thermoautotrophicum has been partially purified by ion-exchange and gel-filtration chromatography. Its molecular weight is estimated to be 100,000 by the latter step. Unlike all previously studied ribonucleotide reductases, the enzyme does not employ dithiol compounds such as dithiothreitol as artificial electron donors in in vitro assays. Inhibition of the enzyme by S-adenosylmethionine, oxygen, and azide further distinguishes it from the Escherichia coli anaerobic enzyme, the iron- and manganese-containing, and the adenosylcobalamin-dependent enzymes. Our preliminary results suggest that this enzyme has an activation mechanism different from the known classes of ribonucleotide reductases.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Sze IS,McFarlan SC,Spormann A,Hogenkamp HP,Follmann Hdoi
10.1016/0006-291x(92)90705-psubject
Has Abstractpub_date
1992-04-30 00:00:00pages
1101-7issue
2eissn
0006-291Xissn
1090-2104pii
0006-291X(92)90705-Pjournal_volume
184pub_type
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