title: Purification and characterization of ferredoxin from Hydrogenobacter thermophilus strain TK-6.
abstract: Ferredoxin was purified from cells of Hydrogenobacter thermophilus strain TK-6. Purification was performed aerobically by the addition of octyl-beta-glucoside to the buffers. The purified ferredoxin had a molecular mass of 13,000 and contained a [4F3-4S] 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 Archaebacteria.
authors.affiliation: Department of Biotechnology, University of Tokyo, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Ishii
authors.forename: Y
authors.initials: Y
authors.lastname: Ueda
authors.forename: K S
authors.initials: KS
authors.lastname: Yoon
authors.forename: Y
authors.initials: Y
authors.lastname: Igarashi
authors.forename: T
authors.initials: T
authors.lastname: Kodama
mesh_terms: D000595:Amino Acid Sequence; D001420:Bacteria, Aerobic / Q000737:chemistry*; D002850:Chromatography, Gel; D005288:Ferredoxins / Q000737:chemistry / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013053:Spectrophotometry / Q000379:methods; D013056:Spectrophotometry, Ultraviolet
chemical_list: D005288:Ferredoxins