(I,0) Mixed-Valence State of a Diiron Complex with Pertinence to the [FeFe]-Hydrogenase Active Site: An IR, EPR, and Computational Study-Reference-Cited by-同舟云学术

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(I,0) Mixed-Valence State of a Diiron Complex with Pertinence to the [FeFe]-Hydrogenase Active Site: An IR, EPR, and Computational Study

Published:2009-11-04 Issue:23 Volume:48 Page:10883-10885
ISSN:0020-1669
Container-title:Inorganic Chemistry
language:en
Short-container-title:Inorg. Chem.

Author:

Singh Pradyumna S.¹,Rudbeck Hans Christian¹,Huang Ping¹,Ezzaher Salah¹,Eriksson Lars²,Stein Matthias³,Ott Sascha¹,Lomoth Reiner¹

Affiliation:

1. Department of Photochemistry and Molecular Science, The Ångström Laboratories, Uppsala University, BOX 532, 751 20 Uppsala, Sweden

2. Department of Physical, Inorganic and Structural Chemistry, Stockholm University, 106 91 Stockholm, Sweden

3. EML Research gGmbH, Molecular and Cellular Modeling, Schloss-Wolfsbrunnenweg 33, 69118 Heidelberg, Germany

Publisher

American Chemical Society (ACS)

Subject

Inorganic Chemistry,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ic9016454

Reference21 articles.

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

2. Solar water-splitting into H2 and O2: design principles of photosystem II and hydrogenases

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

4. Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center

5. The structure and mechanism of iron-hydrogenases

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