Abstract
Cytochrome aa3 serves as a terminal oxidase in the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. A procedure for its isolation is described. The purified preparation consists of only one major polypeptide of 38 kDa apparent molecular mass. The enzyme contains two heme α molecules with midpoint potentials of + 220 and + 370 mV, respectively. The copper content is at least 2 Cu/aa3. It has only negligible capacity to oxidize cytochrome c, but rather serves as an oxidase for reduced caldariella quinone as present in the membrane of Sulfolobus.
Original language | English |
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Journal | FEBS Letters |
Volume | 244 |
Issue number | 2 |
Pages (from-to) | 451-455 |
Number of pages | 5 |
ISSN | 0014-5793 |
DOIs | |
Publication status | Published - 27.02.1989 |
Research Areas and Centers
- Academic Focus: Center for Infection and Inflammation Research (ZIEL)