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Properties of a thermostable 4Fe‐ferredoxin from the hyperthermophilic bacterium Thermotoga maritima
A ferredoxin has been purified from one of the most ancient and the most thermophilic bacteria known, Thermotoga maritima, which grous up to 90°C. The reduced protein (Mr approx. 6300) contains a single S = 1 2 [4Fe 4S]1+ cluster with complete cysteinyl ligation, and was unaffected after incubation...
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Published in: | FEMS microbiology letters 1994-08, Vol.121 (2), p.165-169 |
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description | A ferredoxin has been purified from one of the most ancient and the most thermophilic bacteria known, Thermotoga maritima, which grous up to 90°C. The reduced protein (Mr approx. 6300) contains a single S = 1 2 [4Fe 4S]1+ cluster with complete cysteinyl ligation, and was unaffected after incubation at 95°C for 12 h. It functioned as an electron carrier for T. maritima pyruvate oxidoreductase. Remarkably, the properties and amino acid sequence of this hyperthermophilic bacterial protein are much more similar to those of ferredoxins from hyperthermophilic archaea, rather than ferredoxins from mesophilic and moderately thermophilic bacteria. |
doi_str_mv | 10.1111/j.1574-6968.1994.tb07094.x |
format | article |
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source | Alma/SFX Local Collection |
subjects | Amino Acid Sequence Bacteriology Biological and medical sciences Evolution Fermentation Ferredoxins - chemistry Ferredoxins - isolation & purification Fundamental and applied biological sciences. Psychology Gram-Negative Anaerobic Bacteria - chemistry Hyperthermophilic Archaea Metabolism. Enzymes Microbiology Molecular Sequence Data Thermostability Thermotoga maritima |
title | Properties of a thermostable 4Fe‐ferredoxin from the hyperthermophilic bacterium Thermotoga maritima |
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