{'fraction_non_alphanumeric': 0.01618578465869106, 'fraction_numerical': 0.00422237860661506, 'mean_word_length': 5.32, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 1, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Regulation of an in vivo metal-exchangeable superoxide dismutase from Propionibacterium shermanii exhibiting activity with different metal cofactors.

The anaerobic, but aerotolerant Propionibacterium freudenreichii sp. shermanii contains a single superoxide dismutase [EC 1.15.1.1.] exhibiting comparable activity with iron or manganese as metal cofactor. The formation of superoxide dismutase is not depending on the supplementation of iron or manganese to the culture medium. Even in the absence of these metals the protein is built in comparable amounts. Bacteria grown in the absence of iron and manganese synthesize a superoxide dismutase with very low activity which had incorporated copper. If the medium was also depleted of copper, cobalt was incorporated, leading to an enzymically inactive form. In the absence of cobalt an enzymically inactive superoxide dismutase was built with unknown metal contents. Upon aeration the amount of superoxide dismutase activity increased continuously up to 9 h, due to a de novo synthesis of the protein. This superoxide dismutase had incorporated iron into the active centre. The superoxide dismutase of Propionibacterium shermanii is able to form a much wider variety of complexes with trace metal ions in vivo than previously recognized, leading to the hypothesis that the original function of these proteins was the binding of cytoplasmic trace metals present in excess.