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Purification of the nickel protein carbon monoxide dehydrogenase of Clostridium thermoaceticum
Author(s) -
Diekert Gabriele,
Ritter Maria
Publication year - 1983
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(83)80338-x
Subject(s) - carbon monoxide dehydrogenase , carbon monoxide , nickel , chemistry , enzyme , dehydrogenase , biochemistry , clostridium , biology , organic chemistry , catalysis , bacteria , genetics
The carbon monoxide dehydrogenase was purified from Clostridium thermoaceticum to apparent homogeneity. The 120‐fold purified enzyme with app. M r 250000 had a nickel content of 10 ± 2 μmol Ni/protein.