5,10-Methenyltetrahydromethanopterin hydrogenase
5,10-methenyltetrahydromethanopterin hydrogenase | |||||||||
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Identifiers | |||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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H2-forming N5,N10-methylene-tetrahydromethanopterin dehydrogenase | |||||||||
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Identifiers | |||||||||
Symbol | HMD | ||||||||
Pfam | PF03201 | ||||||||
InterPro | IPR004889 | ||||||||
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The 5,10-methenyltetrahydromethanopterin hydrogenase (or Hmd), the so-called iron-sulfur cluster-free hydrogenase, is an
Enzyme function
Methanogens rely on such enzymes to
Among the hydrogenase family of enzymes, Hmd is unique in that it does not directly reduce CO2 to CH4. The natural substrate of the enzyme is the organic compound methenyltetrahydromethanopterin.[2] The organic compound includes a methenyl group bound to two tertiary amides. The methenyl group originated as CO2 before being incorporated into the substrate, which is catalytically reduced by H2 to methylenetetrahydromethanopterin as shown.[3] Eventually the methylene group is further reduced and released as a molecule of methane.
The
Chemical and physical properties
Hmd holoenzyme
The Hmd holoenzyme includes the protein
The enzymatic activity of the enzyme is lost upon exposure to sunlight or UV. Photolysis causes the release of an iron atom and two molecules of carbon monoxide. In the holoenzyme the Fe and CO molecules are found associated with a 542 Da cofactor.[4]
Hmd iron-containing cofactor
The iron-containing co-factor is found tightly associated with the protein. It can be released upon
As mentioned, irradiation of the co-factor with UV light results in the loss of CO and Fe. In addition the 542 Da compound can be further degraded by a
Although the mechanism by which Hmd acts is unknown, the iron-containing cofactor is in part responsible for the catalytic activity. High concentrations of CO inhibit the enzyme as well, implicating iron as the center of catalysis. It has been proposed that the iron functions to bind H2 and the substrate methenyltetrahydromethanopterin, organizing these two reactants in close proximity.[1]
References
Further reading
- Blaut M (1994). "Metabolism of methanogens". Antonie van Leeuwenhoek. 66 (1–3): 187–208. S2CID 23706408.
- Karyakin AA, Varfolomeev SD (1986). "Catalytic Properties of Hydrogenases". Russian Chemical Reviews. 55 (9): 867–882. .