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J. Biochem, 1992, Vol. 112, No. 6 792-795
© 1992 Japanese Biochemical Society

research-article

Purification and Characterization of a 7Fe Ferredoxin from a Thermophilic Hydrogen-Oxidizing Bacterium, Bacillus schlegelii1

Shigekhi Aono, Himmichi Kurita, Seiichi Uno and Ichiro Okura

Department of Bioengineering, Tokyo Institute of Technology Nagatsuta, Midori-ku Yokohama, Kanagawa 227

A ferredoxin (Fd) was purified from a thermophilic hydrogen-oxidizing bacterium, Bacillus schlegelii. This ferredoxin was a monomer with apparent molecular weight of 13,000 and contained 7 mol Fe/mol ferredoxin. The oxidized ferredoxin showed the characteristic EPR spectrum for [3Fe-4S]1+ (1.2 spin/mol Fd). This signal disappeared upon reduction with dithionite and new signals due to [3Fe-4S]0 and [4Fe-48]1+ (0.7 spin/mol Fd) appeared. The qnantitation of EPR signals and the iron content reveal that B. schlegelii ferredoxin contains one [3Fe-45]1+/0 and one [4Fe-48]2+/1+ cluster. The ferredoxin has the characteristic distribution of cysteinee (-Cys8-X7-Cys16-X3-Cys20-Pro-) for 7Fe ferredoxins in the N-terminus.

1This work was supported by a Grant-in-Aid for Scientific Research (No. 03463084) from the Ministry of Education, Science and Culture of Japan.


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