Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The iron-sulfur cluster-free hydrogenase (Hmd) is a metalloenzyme with a novel iron binding motif.

The Journal of biological chemistry - 13 Oct 2006

Korbas Malgorzata, Vogt Sonja, Meyer-Klaucke Wolfram, Bill Eckhard, Lyon Erica J, Thauer Rudolf K, Shima Seigo

Abstract excerpt

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 isolated enzyme from Methanothermobacter marburgensis (mHmd) and of the active, reconstituted enzyme from Methanocaldococcus jannaschii (jHmd) revealed the presence of mononuclear iron with two CO, one sulfur and one or two N/O in...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Archaeal Proteins
Share to Carbon

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Carbon Monoxide

Share to Hydrogenase

Share to Iron-Sulfur Proteins

Share to Ligands

Share to Thermodynamics

Source

Identifiers

PMID: 16887798
DOI: 10.1074/jbc.M605306200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The iron-sulfur cluster-free hydrogenase (Hmd) is a metalloenzyme with a novel iron binding motif.PMID 16887798Read ↗

Class III hybrid cluster protein homodimeric architecture shows evolutionary relationship with Ni, Fe-carbon monoxide dehydrogenases.Semantic proximity Read ↗

The role of geochemistry and energetics in the evolution of modern respiratory complexes from a proton-reducing ancestor.Semantic proximity Read ↗

Phenotypic evidence that the function of the [Fe]-hydrogenase Hmd in Methanococcus maripaludis requires seven hcg (hmd co-occurring genes) but not hmdII.Semantic proximity Read ↗

Microbial hydrogen splitting in the presence of oxygen.Semantic proximity Read ↗

The effect of a C298D mutation in CaHydA [FeFe]-hydrogenase: Insights into the protein-metal cluster interaction by EPR and FTIR spectroscopic investigation.Semantic proximity Read ↗

The oxidative inactivation of FeFe hydrogenase reveals the flexibility of the H-cluster.Semantic proximity Read ↗

[FeFe]- and [NiFe]-hydrogenase diversity, mechanism, and maturation.Semantic proximity Read ↗

Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation.Semantic proximity Read ↗

CO synthesized from the central one-carbon pool as source for the iron carbonyl in O2-tolerant [NiFe]-hydrogenase.Semantic proximity Read ↗

Mutational and structural studies of (βα)8-barrel fold methylene-tetrahydropterin reductases utilizing a common catalytic mechanism.Semantic proximity Read ↗

Genetic, Biochemical, and Molecular Characterization of Methanosarcina barkeri Mutants Lacking Three Distinct Classes of Hydrogenase.Semantic proximity Read ↗

[FeFe] hydrogenases and their evolution: a genomic perspective.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.