K β Detected High‐Resolution XANES of Fe II and Fe III Models of the 2‐His‐1‐Carboxylate Motif: Analysis of the Carboxylate Binding Mode-Reference-Cited by-同舟云学术

K β Detected High‐Resolution XANES of Fe II and Fe III Models of the 2‐His‐1‐Carboxylate Motif: Analysis of the Carboxylate Binding Mode

Published:2012-01-30 Issue:10 Volume:2012 Page:1589-1597
ISSN:1434-1948
Container-title:European Journal of Inorganic Chemistry
language:en
Short-container-title:Eur. J. Inorg. Chem.

Author:

Mijovilovich Ana¹,Hayashi Hisashi²,Kawamura Naomi³,Osawa Hitoshi³,Bruijnincx Pieter C. A.¹,Klein Gebbink Robertus J. M.⁴,de Groot Frank M. F.¹,Weckhuysen Bert M.¹

Affiliation:

1. Inorganic Chemistry and Catalysis Group, Debye Institute for Nanomaterials Science, Utrecht University, Universiteitsweg 99, 3584 CG Utrecht, The Netherlands

2. Japan Women's University, 2‐8‐1 Mejirodai, Bunkyo‐ku, Tokyo 112‐8681, Japan

3. JASRI‐SPring8, 1‐1‐1 Kouto, Sayo, Hyogo 679‐5198, Japan

4. Organic Chemistry and Catalysis Group, Debye Institute for Nanomaterials Science, Utrecht University, Universiteitsweg 99, 3584 CG Utrecht, The Netherlands

Publisher

Wiley

Subject

Inorganic Chemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/ejic.201101075

Reference53 articles.

1. Geometric and Electronic Structure/Function Correlations in Non-Heme Iron Enzymes

2. Dioxygen Activation at Mononuclear Nonheme Iron Active Sites: Enzymes, Models, and Intermediates

3. Mononuclear non-heme iron enzymes with the 2-His-1-carboxylate facial triad: recent developments in enzymology and modeling studies

4. Solving the riddle of the intradiol and extradiol catechol dioxygenases: how do enzymes control hydroperoxide rearrangements?

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