Purification and properties of an F₄₂₀H₂ dehydrogenase from Methanosarcina mazei Gö1

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• 作者：Abken ; Hans-Jö ; rg ; Deppenmeier ; Uwe
• 关键词：Archaea ; Methanogenesis ; Energy conservation ; Quinone ; Heterodisulfide reductase ; Cytochrome ; CoM-SH ; 2-mercaptoethanesulfonate ; F₄₂₀ ; (N-l-lactyl-γ ; -l-glutamyl)-l-glutamic acid phosphodiester of 7 ; 8-didemethyl-8-hydroxy-5-deazariboflavin-5
• 刊名：FEMS Microbiology Letters
• 出版年：1997
• 出版时间：September 15, 1997
• 年：1997
• 卷：154
• 期：2
• 页码：231-237
• 全文大小：592 K

文摘

The F₄₂₀H₂ dehydrogenase is part of the energy-conserving F₄₂₀H₂:heterodisulfide oxidoreductase system in Methanosarcina mazei Gö1. The enzyme was purified 75-fold to apparent homogeneity from washed membranes. The molecular mass as determined by both native gel electrophoresis and gel filtration was 115 000. The purified enzyme was composed of five different polypeptides with molecular masses of 40, 37, 22, 20, and 16 kDa and contained 7 mol S²⁻ and 7 mol Fe. The specific activity was 17 U mg protein⁻¹ (apparent V_max) using F₄₂₀H₂ as electron donor (K_m