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Structure-function relationships in [FeFe]-hydrogenase active site maturation.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2012 Apr 20; Vol. 287 (17), pp. 13532-40. Date of Electronic Publication: 2012 Mar 02. - Publication Year :
- 2012
-
Abstract
- Since the discovery that, despite the active site complexity, only three gene products suffice to obtain active recombinant [FeFe]-hydrogenase, significant light has been shed on this process. Both the source of the CO and CN(-) ligands to iron and the assembly site of the catalytic subcluster are known, and an apo structure of HydF has been published recently. However, the nature of the substrate(s) for the synthesis of the bridging dithiolate ligand to the subcluster remains to be established. From both spectroscopy and model chemistry, it is predicted that an amine function in this ligand plays a central role in catalysis, acting as a base in the heterolytic cleavage of hydrogen.
- Subjects :
- Algorithms
Biochemistry methods
Catalysis
Catalytic Domain
Chlamydomonas metabolism
Escherichia coli Proteins metabolism
Giardia metabolism
Hydrogen chemistry
Ligands
Models, Chemical
Models, Molecular
Molecular Conformation
Recombinant Proteins chemistry
Spectrophotometry methods
Structure-Activity Relationship
Thermotoga maritima metabolism
Trans-Activators metabolism
Hydrogenase chemistry
Iron-Sulfur Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1083-351X
- Volume :
- 287
- Issue :
- 17
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 22389497
- Full Text :
- https://doi.org/10.1074/jbc.R111.310797