The iron-sulfur cluster-free hydrogenase (Hmd) is a metalloenzyme with a novel iron binding motif
M Korbas, S Vogt, W Meyer-Klaucke, E Bill… - Journal of biological …, 2006 - ASBMB
The iron-sulfur cluster-free hydrogenase (Hmd) from methanogenic archaea harbors an iron-
containing cofactor of yet unknown structure. X-ray absorption spectroscopy of the active, as …
containing cofactor of yet unknown structure. X-ray absorption spectroscopy of the active, as …
Mössbauer studies of the iron− sulfur cluster-free hydrogenase: the electronic state of the mononuclear Fe active site
S Shima, EJ Lyon, RK Thauer… - Journal of the American …, 2005 - ACS Publications
The iron− sulfur cluster-free hydrogenase (Hmd) from methanogenic archaea harbors an
iron-containing, light-sensitive cofactor of still unknown structure as prosthetic group. The …
iron-containing, light-sensitive cofactor of still unknown structure as prosthetic group. The …
The crystal structure of the apoenzyme of the iron–sulphur cluster-free hydrogenase
O Pilak, B Mamat, S Vogt, CH Hagemeier… - Journal of molecular …, 2006 - Elsevier
The iron–sulphur cluster-free hydrogenase (Hmd, EC 1.12. 98.2) from methanogenic
archaea is a novel type of hydrogenase that tightly binds an iron-containing cofactor. The …
archaea is a novel type of hydrogenase that tightly binds an iron-containing cofactor. The …
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 …
A third type of hydrogenase catalyzing H2 activation
S Shima, RK Thauer - The chemical record, 2007 - Wiley Online Library
The activation of molecular hydrogen is of interest both from a chemical and biological
viewpoint. The covalent bond of H2 is strong (436 kJ mol− 1). Its cleavage is catalyzed by …
viewpoint. The covalent bond of H2 is strong (436 kJ mol− 1). Its cleavage is catalyzed by …
Characterization of the Fe site in iron− sulfur cluster-free hydrogenase (Hmd) and of a model compound via nuclear resonance vibrational spectroscopy (NRVS)
We have used 57Fe nuclear resonance vibrational spectroscopy (NRVS) to study the iron
site in the iron− sulfur cluster-free hydrogenase Hmd from the methanogenic archaeon …
site in the iron− sulfur cluster-free hydrogenase Hmd from the methanogenic archaeon …
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 …
Structure and mechanism of iron-only hydrogenases
JW Peters - Current opinion in structural biology, 1999 - Elsevier
The recent elucidation of the structures of iron-only hydrogenases from the microorganisms
Clostridium pasteurianum and Desulfovibrio desulfuricans has revealed that the presumed …
Clostridium pasteurianum and Desulfovibrio desulfuricans has revealed that the presumed …
The iron centre of the cluster-free hydrogenase (Hmd): low-spin Fe (II) or low-spin Fe (0)?
X Wang, Z Li, X Zeng, Q Luo, DJ Evans… - Chemical …, 2008 - pubs.rsc.org
The iron centre of the cluster -free hydrogenase ( Hmd ): low-spin Fe(ii) or low-spin Fe(0) ? -
Chemical Communications (RSC Publishing) DOI:10.1039/B805262J Royal Society of …
Chemical Communications (RSC Publishing) DOI:10.1039/B805262J Royal Society of …