Embedding a ruthenium-based structural mimic of the [Fe]-hydrogenase cofactor into papain

Embedding a ruthenium-based structural mimic of the [Fe]-hydrogenase cofactor into papain

We describe the synthesis of the ruthenacyclic carbamoyl complexes [Ru(2-NHC(O)C5H3NMe)(CO)2( o,o-Me2-C6H3S)(L)] (L = H2O or MeCN), which have a labile water or acetonitrile ligand at their sixth coordination sites. Steric bulk around the ruthenium center is essential in preventing isomerization and...

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Bibliographic Details
Main Authors: Barik, Chandan Kr, Ganguly, Rakesh, Li, Yongxin, Przybylski, Cédric, Salmain, Michèle, Leong, Weng Kee
Other Authors: School of Physical and Mathematical Sciences
Format: Article
Language:English
Published: 2020
Subjects:
Science::Chemistry
Science::Chemistry::Inorganic chemistry
Ruthenium
[Fe]- Hydrogenase
Online Access:https://hdl.handle.net/10356/136695
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Institution: Nanyang Technological University
Language: English
Description
Summary:We describe the synthesis of the ruthenacyclic carbamoyl complexes [Ru(2-NHC(O)C5H3NMe)(CO)2( o,o-Me2-C6H3S)(L)] (L = H2O or MeCN), which have a labile water or acetonitrile ligand at their sixth coordination sites. Steric bulk around the ruthenium center is essential in preventing isomerization and dimerization, and embedding within papain can be achieved via coordination of its sole free cysteine residue. The observed chemistry parallels that of the natural [Fe]-hydrogenase.

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