The Iron-Sulfur Cluster-free Hydrogenase (Hmd) Is a Metalloenzyme with a Novel Iron Binding Motif
Open Access
- 1 October 2006
- journal article
- Published by Elsevier
- Vol. 281 (41) , 30804-30813
- https://doi.org/10.1074/jbc.m605306200
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- The Crystal Structure of the Apoenzyme of the Iron–Sulphur Cluster-free HydrogenaseJournal of Molecular Biology, 2006
- The structure of the Ni–Fe site in the isolated HoxC subunit of the hydrogen‐sensing hydrogenase from Ralstonia eutrophaFEBS Letters, 2005
- Structural differences between the ready and unready oxidized states of [NiFe] hydrogenasesJBIC Journal of Biological Inorganic Chemistry, 2005
- Direct interaction of coenzyme M with the active‐site Fe–S cluster of heterodisulfide reductaseFEBS Letters, 2005
- Hydrogenases: active site puzzles and progressCurrent Opinion in Chemical Biology, 2004
- Studies on the catalytic mechanism of H2-forming methylenetetrahydromethanopterin dehydrogenase: para-ortho H2 conversion rates in H2O and D2OJBIC Journal of Biological Inorganic Chemistry, 1996
- Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigasNature, 1995
- Number of relevant independent points in x-ray-absorption fine-structure spectraPhysical Review B, 1993
- N5,N10‐Methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum has hydrogenase activityFEBS Letters, 1990
- Absolute energy calibration of X-ray radiation from synchrotron sourcesJournal of Applied Crystallography, 1985