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Isolation, characterization and crystallization of an iron-superoxide dismutase from the crenarchaeon Sulfolobus acidocaldarius.
FEMS Microbiol Lett 1996; 138(1):65-70FM

Abstract

An iron containing superoxide dismutase from the cytosol of the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius (DSM 639) has been purified to electrophoretic homogeneity. It comprises at least 11% of the cytosolic protein. The isolated protein consists of two identical subunits with an apparent molecular mass of 22.4 kDa. It contains one iron atom per dimer. The protein shows the typical EPR spectrum of a S = 3/2, rhombic high-spin iron center. It is extremely resistant against thermal and chemical denaturation. Simultaneous treatment with heat and detergent resulted in the conversion into a more active tetrameric form. Similar enzymes appear to be present in the cytosol of other members of the Sulfolobaceae. The dimeric form of the protein from S. acidocaldarius has been crystallized.

Authors+Show Affiliations

Institut für Biochemie, Medizinische Universität zu Lübeck, Germany.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

8674972

Citation

Kardinahl, S, et al. "Isolation, Characterization and Crystallization of an Iron-superoxide Dismutase From the Crenarchaeon Sulfolobus Acidocaldarius." FEMS Microbiology Letters, vol. 138, no. 1, 1996, pp. 65-70.
Kardinahl S, Schmidt CL, Petersen A, et al. Isolation, characterization and crystallization of an iron-superoxide dismutase from the crenarchaeon Sulfolobus acidocaldarius. FEMS Microbiol Lett. 1996;138(1):65-70.
Kardinahl, S., Schmidt, C. L., Petersen, A., & Schäfer, G. (1996). Isolation, characterization and crystallization of an iron-superoxide dismutase from the crenarchaeon Sulfolobus acidocaldarius. FEMS Microbiology Letters, 138(1), pp. 65-70.
Kardinahl S, et al. Isolation, Characterization and Crystallization of an Iron-superoxide Dismutase From the Crenarchaeon Sulfolobus Acidocaldarius. FEMS Microbiol Lett. 1996 Apr 15;138(1):65-70. PubMed PMID: 8674972.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Isolation, characterization and crystallization of an iron-superoxide dismutase from the crenarchaeon Sulfolobus acidocaldarius. AU - Kardinahl,S, AU - Schmidt,C L, AU - Petersen,A, AU - Schäfer,G, PY - 1996/4/15/pubmed PY - 1996/4/15/medline PY - 1996/4/15/entrez SP - 65 EP - 70 JF - FEMS microbiology letters JO - FEMS Microbiol. Lett. VL - 138 IS - 1 N2 - An iron containing superoxide dismutase from the cytosol of the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius (DSM 639) has been purified to electrophoretic homogeneity. It comprises at least 11% of the cytosolic protein. The isolated protein consists of two identical subunits with an apparent molecular mass of 22.4 kDa. It contains one iron atom per dimer. The protein shows the typical EPR spectrum of a S = 3/2, rhombic high-spin iron center. It is extremely resistant against thermal and chemical denaturation. Simultaneous treatment with heat and detergent resulted in the conversion into a more active tetrameric form. Similar enzymes appear to be present in the cytosol of other members of the Sulfolobaceae. The dimeric form of the protein from S. acidocaldarius has been crystallized. SN - 0378-1097 UR - https://www.unboundmedicine.com/medline/citation/8674972/Isolation_characterization_and_crystallization_of_an_iron_superoxide_dismutase_from_the_crenarchaeon_Sulfolobus_acidocaldarius_ L2 - https://academic.oup.com/femsle/article-lookup/doi/10.1111/j.1574-6968.1996.tb08136.x DB - PRIME DP - Unbound Medicine ER -