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Literature DB >> 16391742

An insight into the protonation property of a diiron azadithiolate complex pertinent to the active site of Fe-only hydrogenases.

Weibing Dong¹, Mei Wang, Xiaoyang Liu, Kun Jin, Guanghua Li, Fujun Wang, Licheng Sun.

Abstract

Protonation of [{(mu-SCH2)2N(C6H4-p-NO2)}{Fe(CO)2(PMe3)}2] in the presence of 4 equiv. of HOTf afforded two species, a micro-hydride diiron complex, the molecular structure of which was crystallographically characterized, and a micro-S-protonated species, which was readily deprotonated in the presence of pyridine.

Entities: Chemical

Year: 2005 PMID： 16391742 DOI： 10.1039/b513270c

Source DB: PubMed Journal: Chem Commun (Camb) ISSN： 1359-7345 Impact factor: 6.222

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Cited

13 in total

1. Unsaturated, mixed-valence diiron dithiolate model for the H(ox) state of the [FeFe] hydrogenase.

Authors: Aaron K Justice; Thomas B Rauchfuss; Scott R Wilson
Journal: Angew Chem Int Ed Engl Date: 2007 Impact factor: 15.336

2. The oxidative inactivation of FeFe hydrogenase reveals the flexibility of the H-cluster.

Authors: Vincent Fourmond; Claudio Greco; Kateryna Sybirna; Carole Baffert; Po-Hung Wang; Pierre Ezanno; Marco Montefiori; Maurizio Bruschi; Isabelle Meynial-Salles; Philippe Soucaille; Jochen Blumberger; Hervé Bottin; Luca De Gioia; Christophe Léger
Journal: Nat Chem Date: 2014-03-16 Impact factor: 24.427

Review 3. Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides.

Authors: David Schilter; James M Camara; Mioy T Huynh; Sharon Hammes-Schiffer; Thomas B Rauchfuss
Journal: Chem Rev Date: 2016-06-29 Impact factor: 60.622

4. Favorable Protonation of the (μ-edt)[Fe(2)(PMe(3))(4)(CO)(2)(H-terminal)](+) Hydrogenase Model Complex Over Its Bridging μ-H Counterpart: A Spectroscopic and DFT Study.

Authors: Mary Grace I Galinato; C Matthew Whaley; Dean Roberts; Peng Wang; Nicolai Lehnert
Journal: Eur J Inorg Chem Date: 2011-03 Impact factor: 2.524

5. Role of the azadithiolate cofactor in models for [FeFe]-hydrogenase: novel structures and catalytic implications.

Authors: Matthew T Olsen; Thomas B Rauchfuss; Scott R Wilson
Journal: J Am Chem Soc Date: 2010-11-29 Impact factor: 15.419

6. Vibrational analysis of the model complex (mu-edt)[Fe(CO)(3)](2) and comparison to iron-only hydrogenase: the activation scale of hydrogenase model systems.

Authors: Mary Grace I Galinato; C Matthew Whaley; Nicolai Lehnert
Journal: Inorg Chem Date: 2010-04-05 Impact factor: 5.165

An insight into the protonation property of a diiron azadithiolate complex pertinent to the active site of Fe-only hydrogenases.

1. Unsaturated, mixed-valence diiron dithiolate model for the H(ox) state of the [FeFe] hydrogenase.

2. The oxidative inactivation of FeFe hydrogenase reveals the flexibility of the H-cluster.

Review 3. Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides.

4. Favorable Protonation of the (μ-edt)[Fe(2)(PMe(3))(4)(CO)(2)(H-terminal)](+) Hydrogenase Model Complex Over Its Bridging μ-H Counterpart: A Spectroscopic and DFT Study.

5. Role of the azadithiolate cofactor in models for [FeFe]-hydrogenase: novel structures and catalytic implications.

6. Vibrational analysis of the model complex (mu-edt)[Fe(CO)(3)](2) and comparison to iron-only hydrogenase: the activation scale of hydrogenase model systems.

7. Diiron Azamonothiolates via Scission of Dithiadiazacyclooctanes by Iron Carbonyls.

8. Studies on the Condensation Pathway to and Properties of Diiron Azadithiolate Carbonyls.

9. Desymmetrized Diiron Azadithiolato Carbonyls: A Step Toward Modeling the Iron-Only Hydrogenases.

10. [μ-3-(Methyl-sulfan-yl)benzene-1,2-di-thiol-ato-1:2κ(4) S,S':S,S']bis-[tri-carbonyl-iron(I)].