METAL SULPHUR COMPLEXES FOR MODELLING OF NITROGENASE ENZYMES

Document Type : Original Article

Authors

Faculty of Education, Tanta University.

Abstract

ABSTRACT
A new pyS4 and pyN2H2S2-based iron and ruthenium complex have been
synthesized and characterized in order to bind nitrogenase-relevant small molecules.
These fragments were found to bind and stabilize the hydrazine small molecule
which is a very important step in the nitrogenase fixation cycle. X-ray structural
analysis of the hydrazine complexes deserve special interest because all types of
hydrazine hydrogen atoms are involved in a system of inter- and intramolecular
NH···S and NH···N hydrogen bonding with the sulfur donors (thiolate, thioether) as
well as the solvate hydrazine N atoms.

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