The binuclear cluster of [FeFe] hydrogenase is formed with sulfur donated by cysteine of an [Fe(Cys)(CO)₂(CN)] organometallic precursor

The enzyme [FeFe]-hydrogenase (HydA1) contains a unique 6-iron cofactor, the H-cluster, that has unusual ligands to an Fe–Fe binuclear subcluster: CN⁻, CO, and an azadithiolate (adt) ligand that provides 2 S bridges between the 2 Fe atoms. In cells, the H-cluster is assembled by a collection of 3 ma...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2019-10, Vol.116 (42), p.20850-20855
Hauptverfasser:	Rao, Guodong, Pattenaude, Scott A., Alwan, Katherine, Blackburn, Ninian J., Britt, R. David, Rauchfuss, Thomas B.
Format:	Artikel
Sprache:	eng
Schlagworte:	Assembly Bacterial Proteins - chemistry Bacterial Proteins - metabolism Catalysis Catalytic Domain Clusters Couplings Cysteine Cysteine - chemistry Cysteine - metabolism Electron paramagnetic resonance Electron Spin Resonance Spectroscopy Enzymes Fine structure Hydrogenase Hydrogenase - chemistry Infrared spectra Iron Iron - chemistry Iron - metabolism Ligands Maturation Nitrogen atoms Organometallic Compounds - chemistry Organometallic Compounds - metabolism Physical Sciences Precursors Pyruvic acid Resonance Spectrometry Spectroscopy Sulfur Sulfur - chemistry Sulfur - metabolism Ultrastructure X ray absorption
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