Purification and characterization of ferredoxin from hydrogenobacter thermophilus strain TK-6

Abstract

Ferredoxin was purified from cells of Hydrogenohacter thermophilus strain TK-6. Purification was performed aerobically by the addition of octyl-p-glucoside to the buffers. The purified ferredoxin had a molecular mass of 13,000 and contained a [4Fe-4S] cluster. The protein had a long stretch at the N-terminal region; however, the sequence was not similar to the sequences of ferredoxins with a long stretch from Archaehacteria. © 1996, Taylor & Francis Group, LLC. All rights reserved.