The metal‐free hydrogenase from methanogenic archaea: evidence for a bound cofactor
- 21 November 2000
- journal article
- Published by Wiley in FEBS Letters
- Vol. 485 (2-3) , 200-204
- https://doi.org/10.1016/s0014-5793(00)02225-0
Abstract
The hmd gene, which encodes the metal-free hydrogenase in methanogenic archaea, was heterologously expressed in Escherichia coli. The overproduced enzyme was completely inactive. High activity could, however, be induced by the addition of ultrafiltrate from active enzyme denatured in 8 M urea. The active fraction in the ultrafiltrate was heat-labile and migrated on gel filtration columns with an apparent molecular mass well below 1000 Da.Keywords
This publication has 18 references indexed in Scilit:
- Hydrogenation without a Metal Catalyst: An ab Initio Study on the Mechanism of the Metal-Free Hydrogenase from Methanobacterium thermoautotrophicumJournal of the American Chemical Society, 1998
- Remarkable cleavage of molecular hydrogen without the use of metallic catalysts: a theoretical investigationNew Journal of Chemistry, 1998
- Geometry‐Tunable Lewis Acidity of Amidinium Cations and Its Relevance to Redox Reactions of the Thauer Metal‐Free Hydrogenase: A Theoretical StudyAngewandte Chemie International Edition in English, 1997
- Complete Genome Sequence of the Methanogenic Archaeon, Methanococcus jannaschii Science, 1996
- On the Mechanism of Catalysis by a Metal‐Free Hydrogenase from Methanogenic Archaea: Enzymatic Transformation of H2 without a Metal and Its Analogy to the Chemistry of Alkanes in Superacidic SolutionAngewandte Chemie International Edition in English, 1995
- Salt dependence, kinetic properties and catalytic mechanism of N‐formylmethanofuran:tetrahydromethanopterin formyltransferase from the extreme thermophile Methanopyrus kandleriEuropean Journal of Biochemistry, 1992
- H2‐forming methylenetetrahydromethanopterin dehydrogenase, a novel type of hydrogenase without iron‐sulfur clusters in methanogenic archaeaEuropean Journal of Biochemistry, 1992
- Hydrogen‐forming and coenzyme‐F420‐reducing methylene tetrahydromethanopterin dehydrogenase are genetically distinct enzymes in Methanobacterium thermoautotrophicum (Marburg)European Journal of Biochemistry, 1991
- N5,N10‐Methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum has hydrogenase activityFEBS Letters, 1990
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976