TAILIEUCHUNG - Báo cáo khoa học: Purification and characterization of a membrane-bound enzyme complex from the sulfate-reducing archaeon Archaeoglobus fulgidus related to heterodisulfide reductase from methanogenic archaea

Heterodisul®de reductase (Hdr) is a unique disul®de reduc-tase that plays a key role in the energy metabolism of methanogenic archaea. The genome of the sulfate-reducing archaeonArchaeoglobus fulgidusencodes several proteins of unknown function with high sequence similarity to the catalytic subunit of Hdr. Here we report on the puri®cation of a multisubunit membrane-bound enzyme complex from A. | Eur. J. Biochem. 269 1895-1904 2002 FEBS 2002 doi Purification and characterization of a membrane-bound enzyme complex from the sulfate-reducing archaeon Archaeoglobus fulgidus related to heterodisulf de reductase from methanogenic archaea Gerd J. Mander1. Evert C Duin1. Dietmar Linder2 Karl O. Stetter3 and Reiner Hedderich1 . BB. . 1 Max-Planck-Institut fur terrestrische Mikrobiologie Marburg Germany 2Biochemisches Institut Fachbereich Humanmedizin Justus-Liebig-Universitat Giessen Germany 2Lehrstuhl fur Mikrobiologie und Archaeenzentrum Universitat Regensburg Germany Heterodisulfide reductase Hdr is a unique disulfide reductase that plays a key role in the energy metabolism of methanogenic archaea. The genome of the sulfate-reducing archaeon Archaeoglobus fulgidus encodes several proteins of unknown function with high sequence similarity to the catalytic subunit of Hdr. Here we report on the purification of a multisubunit membrane-bound enzyme complex from A. fulgidus that contains a subunit related to the catalytic subunit of Hdr. The purified enzyme is a heme iron-sulfur protein as deduced by UV Vis spectroscopy EPR spectroscopy and the primary structure. It is composed of four different subunits encoded by a putative transcription unit AF499 AF501-AF503 . A fifth protein AF500 encoded by this transcription unit could not be detected in the purified enzyme preparation. Subunit AF502 is closely related to the catalytic subunit HdrD of Hdr from Methanosarcina bark-eri. AF501 encodes a membrane-integral cytochrome and AF500 encodes a second integral membrane protein. AF499 encodes an extracytoplasmic iron-sulfur protein and AF503 encodes an extracytoplasmic c-type cytochrome with three heme c-binding motifs. All of the subunits show high sequence similarity to proteins encoded by the dsr locus of Allochromatium vinosum and to subunits of the Hmc complex from Desulfovibrio vulgaris. The heme groups of the enzyme are rapidly reduced

• Báo cáo khoa học
• Report medicine
• traditional medicine
• scientific reports
• breast cancer
• biological activities
• environmental medicine
• medical knowledge
• medical research
• analysis of cytoplasmic
• oxidation
• Crystal structure
• bacteria
• hemoglobin
• medicine
• cell proliferation
• chemical reaction
• gastric cancer
• hormone medicine
• tumor cells
• biochemical studies