This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3c8y
From Proteopedia
1.39 Angstrom crystal structure of Fe-only hydrogenase
Overview
An X-ray crystallographic refinement of the H-cluster of [FeFe]-hydrogenase from Clostridium pasteurianum has been carried out to close-to atomic resolution and is the highest resolution [FeFe]-hydrogenase presented to date. The 1.39 A, anisotropically refined [FeFe]-hydrogenase structure provides a basis for examining the outstanding issue of the composition of the unique nonprotein dithiolate ligand of the H-cluster. In addition to influencing the electronic structure of the H-cluster, the composition of the ligand has mechanistic implications due to the potential of the bridge-head gamma-group participating in proton transfer during catalysis. In this work, sequential density functional theory optimizations of the dithiolate ligand embedded in a 3.5-3.9 A protein environment provide an unbiased approach to examining the most likely composition of the ligand. Structural, conformational, and energetic considerations indicate a preference for dithiomethylether as an H-cluster ligand and strongly disfavor the dithiomethylammonium as a catalytic base for hydrogen production.
About this Structure
3C8Y is a Single protein structure of sequence from Clostridium pasteurianum. Full crystallographic information is available from OCA.
Reference
Dithiomethylether as a ligand in the hydrogenase h-cluster., Pandey AS, Harris TV, Giles LJ, Peters JW, Szilagyi RK, J Am Chem Soc. 2008 Apr 2;130(13):4533-40. Epub 2008 Mar 7. PMID:18324814 Page seeded by OCA on Thu Apr 24 09:53:22 2008
