UV‐A/blue‐light inactivation of the 'metal‐free'hydrogenase (Hmd) from methanogenic archaea: The enzyme contains functional iron after all
EJ Lyon, S Shima, G Buurman… - European Journal of …, 2004 - Wiley Online Library
H2‐forming methylenetetrahydromethanopterin dehydrogenase (Hmd) is an unusual
hydrogenase present in many methanogenic archaea. The homodimeric enzyme dubbed …
hydrogenase present in many methanogenic archaea. The homodimeric enzyme dubbed …
H2‐forming methylenetetrahydromethanopterin dehydrogenase, a novel type of hydrogenase without iron‐sulfur clusters in methanogenic archaea
C Zirngibl, W Van Dongen, B Schwörer… - European Journal of …, 1992 - Wiley Online Library
A novel hydrogenase has recently been found in methanogenic archaea. It catalyzes the
reversible dehydrogenation of methylenetetrahydromethanopterin (CH2─ H4MPT) to …
reversible dehydrogenation of methylenetetrahydromethanopterin (CH2─ H4MPT) to …
Carbon Monoxide as an Intrinsic Ligand to Iron in the Active Site of the Iron−Sulfur-Cluster-Free Hydrogenase H2-Forming Methylenetetrahydromethanopterin …
EJ Lyon, S Shima, R Boecher, RK Thauer… - Journal of the …, 2004 - ACS Publications
The iron− sulfur-cluster-free hydrogenase Hmd (H2-forming
methylenetetrahydromethanopterin dehydrogenase) from methanogenic archaea has …
methylenetetrahydromethanopterin dehydrogenase) from methanogenic archaea has …
[HTML][HTML] The metal-free hydrogenase from methanogenic archaea: evidence for a bound cofactor
G Buurman, S Shima, RK Thauer - FEBS letters, 2000 - Elsevier
The hmd gene, which encodes the metal-free hydrogenase in methanogenic archaea, was
heterologously expressed in Escherichia coli. The overproduced enzyme was completely …
heterologously expressed in Escherichia coli. The overproduced enzyme was completely …
Activation of dihydrogen without transition metals
A Berkessel - Current Opinion in Chemical Biology, 2001 - Elsevier
The metal-free hydrogenase from methanogenic archaea (Hmd) is a unique enzyme: it
catalyzes the reaction of its substrate, methenyl-tetrahydromethanopterin, with molecular …
catalyzes the reaction of its substrate, methenyl-tetrahydromethanopterin, with molecular …
Evidence for acyl–iron ligation in the active site of [Fe]-hydrogenase provided by mass spectrometry and infrared spectroscopy
S Shima, M Schick, J Kahnt, K Ataka, K Steinbach… - Dalton …, 2012 - pubs.rsc.org
[Fe]-hydrogenase catalyzes the reversible heterolytic cleavage of H2 and stereo-specific
hydride transfer to the substrate methenyltetrahydromethanopterin in methanogenic …
hydride transfer to the substrate methenyltetrahydromethanopterin in methanogenic …
Structure and Function of [Fe]‐Hydrogenase and its Iron–Guanylylpyridinol (FeGP) Cofactor
S Shima, U Ermler - European Journal of Inorganic Chemistry, 2011 - Wiley Online Library
Abstract [Fe]‐hydrogenase functions in the methanogenic pathway of hydrogenotrophic
methanogenic archaea. It catalyzes thereversible reduction of …
methanogenic archaea. It catalyzes thereversible reduction of …
The exchange activities of [Fe] hydrogenase (iron–sulfur-cluster-free hydrogenase) from methanogenic archaea in comparison with the exchange activities of [FeFe] …
S Vogt, EJ Lyon, S Shima, RK Thauer - JBIC Journal of Biological …, 2008 - Springer
Abstract [Fe] hydrogenase (iron–sulfur-cluster-free hydrogenase) catalyzes the reversible
reduction of methenyltetrahydromethanopterin (methenyl-H 4 MPT+) with H 2 to methylene …
reduction of methenyltetrahydromethanopterin (methenyl-H 4 MPT+) with H 2 to methylene …
Molecular biology of microbial hydrogenases
PM Vignais, A Colbeau - Current issues in molecular biology, 2004 - mdpi.com
Hydrogenases (H 2 ases) are metalloproteins. The great majority of them contain iron-sulfur
clusters and two metal atoms at their active center, either a Ni and an Fe atom, the [NiFe]-H 2 …
clusters and two metal atoms at their active center, either a Ni and an Fe atom, the [NiFe]-H 2 …
The Cofactor of the Iron–Sulfur Cluster Free Hydrogenase Hmd: Structure of the Light‐Inactivation Product
S Shima, EJ Lyon, M Sordel‐Klippert… - Angewandte …, 2004 - Wiley Online Library
Hydrogenases are enzymes that catalyze reversible reactions that have H2 as a substrate or
product. There are three classes of hydrogenases which appear not to be structurally and …
product. There are three classes of hydrogenases which appear not to be structurally and …