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Title: Embedding a ruthenium-based structural mimic of the [Fe]-hydrogenase cofactor into papain
Authors: Barik, Chandan Kr
Ganguly, Rakesh
Li, Yongxin
Przybylski, Cédric
Salmain, Michèle
Leong, Weng Kee
Keywords: Science::Chemistry
Science::Chemistry::Inorganic chemistry
Issue Date: 2018
Source: Barik, C. K., Ganguly, R., Li, Y., Przybylski, C., Salmain, M., & Leong, W. K. (2018). Embedding a ruthenium-based structural mimic of the [Fe]-hydrogenase cofactor into papain. Inorganic Chemistry, 57(19), 12206-12212. doi:10.1021/acs.inorgchem.8b01835
Journal: Inorganic Chemistry
Abstract: 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.
ISSN: 0020-1669
DOI: 10.1021/acs.inorgchem.8b01835
Rights: This document is the Accepted Manuscript version of a Published Work that appeared in final form in Inorganic Chemistry, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SPMS Journal Articles

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