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Carbon Monoxide as Intrinsic Ligand to Iron in the Active Site of [Fe]-Hydrogenase

Structural and spectroscopic studies on [Fe]-hydrogenase revealed an active site mononuclear low spin iron coordinated by the Cys176 sulfur, two CO, and the sp2 hybridized nitrogen of a 2-pyridinol compound with back bonding properties similar to those of cyanide. Thus, [Fe]-hydrogenases are endowed with an iron-ligation pattern related to that found in the active site of [NiFe]- and [FeFe]-hydrogenases although the three hydrogenases and the enzymes involved in their posttranslational maturation have evolved independently and although CO and cyanide ligands are not found in any other metallo-enzymes. Obviously, low-spin iron complexed with thiolate(s), CO, and cyanide or a cyanide functional analogue plays an essential role in H2 activation.

Publication details

Print publication date
04 Feb 2009
Copyright year
2009
Print ISBN
978-1-84755-915-9
PDF eISBN
978-1-84755-933-3

From the book series:
Metal Ions in Life Sciences