Open AccessPurification and some properties of the methyl‐CoM reductase of Methanothrix soehngenii
Author(s) -
Jetten Mike S.M.,
Stams Alfons J.M.,
Zehnder Alexander J.B.
Publication year - 1990
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1990.tb03993.x
Subject(s) - chemistry , reductase , enzyme , polyacrylamide gel electrophoresis , chromatography , biochemistry , molecular mass , gel electrophoresis , cofactor
The methyl‐CoM reductase from Methanothrix soehngenii was purified 18‐fold to apparent homogeneity with 50% recovery in three steps. The native molecular mass of the enzyme estimated by gel‐fitration was 280 kDa. SDS‐polyacrylamide gel electrophoresis revealed three protein bands corresponding to M r 63 900, 41 700 and 30 400 Da. The methyl‐coenzyme M reductase constitutes up to 10% of the soluble cell protein. The enzyme has K m apparent values of 23 μM and 2 mM for N ‐7‐mercaptoheptanoylthreonine phosphate (HS‐ HTP = component B ) and methyl‐coenzyme M (CH 3 ?CoM) respectively. At the optimum pH of 7.0 60 nmol of methane were formed per min per mg protein.