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Reactivation of metal‐requiring apoenzymes by phytochelatin—metal complexes
Author(s) -
Thumann Josef,
Grill Erwin,
Winnacker Ernst-L.,
Zenk Meinhart H.
Publication year - 1991
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(91)80763-s
Subject(s) - phytochelatin , metal , copper , zinc , carbonic anhydrase , chemistry , glycine , oxidase test , enzyme , nuclear chemistry , inorganic chemistry , biochemistry , organic chemistry , glutathione , amino acid
The enzymatically inactive, metal‐requiring apoforms of diamino oxidase and of carbonic anhydrase were reactivated by copper‐ and zinc—phytochelatin complexes, respectively. The level and the rate of reactivation effected by metal complexes consisting of poly(γ‐glutamylcysteinyl)glycine as well as by the respective free metal ion were compared. An efficient transfer of zinc and copper from phytochelatin‐complexes to apoenzymes was observed in vitro.