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Single step purification of methylenetetrahydromethanopterin reductase from Methanobacterium thermoautotrophicum by specific binding to Blue Sepharose CL‐6B
Author(s) -
Ma K.,
Thauer R.K.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80972-l
Subject(s) - sepharose , chemistry , biochemistry , stereochemistry , enzyme
Methylenetetrahydromethanopterin reductase from metanogenic archaebacteria catalyzes the reversible reduction of N 5 , N 10 ‐methylenetetrahydro‐methanopterin to N 5 ‐methyltetrahydromethanopterin with reduced coenzyme F 420 as electron donor. The enzyme is involved in methane formation from CO 2 , and in methanoi disproportionation to CO 2 and CH 4 . We report here that the reductase from Methanobacterium thermoautotrophicum specifically binds to Blue Sepharose CL‐6B. Binding was competitive with coenzyme F 420 rather than with NAD, NADP, FAD, FMN, AMP, ADP and ATP. The reductase could also be desorbed with salt. Based on this property an affinity Chromatographie procedure for the purification of the enzyme was developed.