A mononuclear iron carbonyl complex [Fe(μ-bdt)(CO)2(PTA)2] with bulky phosphine ligands: a model for the [FeFe] hydrogenase enzyme active site with an inverted redox potential-Reference-Cited by-同舟云学术

A mononuclear iron carbonyl complex [Fe(μ-bdt)(CO)2(PTA)2] with bulky phosphine ligands: a model for the [FeFe] hydrogenase enzyme active site with an inverted redox potential

Published:2017 Issue:30 Volume:46 Page:10050-10056
ISSN:1477-9226
Container-title:Dalton Transactions
language:en
Short-container-title:Dalton Trans.

Author:

Natarajan M.¹²³⁴,Faujdar H.¹²³⁴,Mobin S. M.⁵⁶⁷⁴^ORCID,Stein M.⁸⁹¹⁰¹¹^ORCID,Kaur-Ghumaan S.¹²³⁴^ORCID

Affiliation:

1. Department of Chemistry

2. University of Delhi

3. Delhi 110007

4. India

5. National Single Crystal X-ray Diffraction Facility

6. IIT Bombay

7. Mumbai 400076

8. Max-Planck-Institute for Dynamics of Complex Technical Systems

9. Molecular Simulations and Design Group

10. 39106 Magdeburg

11. Germany

Abstract

This mononuclear iron complex displays an inverted redox potential and catalyzes hydrogen evolution in acidic solution.

Funder

Max-Planck-Gesellschaft

Publisher

Royal Society of Chemistry (RSC)

Subject

Inorganic Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2017/DT/C7DT01994G

Reference47 articles.

1. Powering the planet: Chemical challenges in solar energy utilization

2. Structural and Functional Analogues of the Active Sites of the [Fe]-, [NiFe]-, and [FeFe]-Hydrogenases

3. X-ray Crystal Structure of the Fe-Only Hydrogenase (CpI) from Clostridium pasteurianum to 1.8 Angstrom Resolution

4. Reactions of [FeFe]-hydrogenase models involving the formation of hydrides related to proton reduction and hydrogen oxidation

5. Mimicking hydrogenases: From biomimetics to artificial enzymes

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