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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sg-ntu-dr.10356-1366952023-02-28T19:25:04Z Embedding a ruthenium-based structural mimic of the [Fe]-hydrogenase cofactor into papain Barik, Chandan Kr Ganguly, Rakesh Li, Yongxin Przybylski, Cédric Salmain, Michèle Leong, Weng Kee School of Physical and Mathematical Sciences Science::Chemistry Science::Chemistry::Inorganic chemistry Ruthenium [Fe]- Hydrogenase 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. ASTAR (Agency for Sci., Tech. and Research, S’pore) Accepted version 2020-01-10T06:40:35Z 2020-01-10T06:40:35Z 2018 Journal Article 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 0020-1669 https://hdl.handle.net/10356/136695 10.1021/acs.inorgchem.8b01835 30198260 2-s2.0-85053309917 19 57 12206 12212 en Inorganic Chemistry 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 https://doi.org/10.1021/acs.inorgchem.8b01835 application/pdf |
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Science::Chemistry Science::Chemistry::Inorganic chemistry Ruthenium [Fe]- Hydrogenase Barik, Chandan Kr Ganguly, Rakesh Li, Yongxin Przybylski, Cédric Salmain, Michèle Leong, Weng Kee Embedding a ruthenium-based structural mimic of the [Fe]-hydrogenase cofactor into papain |
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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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School of Physical and Mathematical Sciences |
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School of Physical and Mathematical Sciences Barik, Chandan Kr Ganguly, Rakesh Li, Yongxin Przybylski, Cédric Salmain, Michèle Leong, Weng Kee |
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Article |
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Barik, Chandan Kr Ganguly, Rakesh Li, Yongxin Przybylski, Cédric Salmain, Michèle Leong, Weng Kee |
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Barik, Chandan Kr |
title |
Embedding a ruthenium-based structural mimic of the [Fe]-hydrogenase cofactor into papain |
title_short |
Embedding a ruthenium-based structural mimic of the [Fe]-hydrogenase cofactor into papain |
title_full |
Embedding a ruthenium-based structural mimic of the [Fe]-hydrogenase cofactor into papain |
title_fullStr |
Embedding a ruthenium-based structural mimic of the [Fe]-hydrogenase cofactor into papain |
title_full_unstemmed |
Embedding a ruthenium-based structural mimic of the [Fe]-hydrogenase cofactor into papain |
title_sort |
embedding a ruthenium-based structural mimic of the [fe]-hydrogenase cofactor into papain |
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2020 |
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https://hdl.handle.net/10356/136695 |
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