## Abstract The properties of a β‐galactosidase from a thermophilic Bacillus have been studied and compared with the properties of the enzyme contained in whole cells and in cells entrapped in a polyacrylamide gel matrix. The partially purified enzyme appears to be optimally active at a temperature
Thermostability and electron transfer activity of the ferredoxin from a thermophilic hydrogen oxidizing bacterium, Bacillus schlegelii
✍ Scribed by Shigetoshi Aono; Norio Fukuda; Ichiro Okura
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 623 KB
- Volume
- 95
- Category
- Article
- ISSN
- 1381-1169
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✦ Synopsis
The Azorobucrer-type 7Fe ferredoxin from Bacillus schlegelii was active as an electron carrier in the reduction system of cyt. c consisting of NADPH, FNR and cytochrome c (cyt. c). The only [ 3Fe_4S] cluster in the Fd molecule acts as the active site for the reduction of cyt. c. The activity of the ferredoxin once increased by IO,20 and 20% by heat treatment at 60,80 and 90°C respectively. The increasing of the activity is caused by the interconversion of the [4Fe-4S] cluster to the [ 3Fe-4S] cluster with increasing of the [ 3Fe_4S] cluster in the concentration.
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