Elucidating light-induced charge accumulation in an artificial analogue of methane monooxygenase enzymes using time-resolved X-ray absorption spectroscopy-Reference-Cited by-同舟云学术

Elucidating light-induced charge accumulation in an artificial analogue of methane monooxygenase enzymes using time-resolved X-ray absorption spectroscopy

Published:2017 Issue:18 Volume:53 Page:2725-2728
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Moonshiram Dooshaye¹²³^ORCID,Picón Antonio¹²³^ORCID,Vazquez-Mayagoitia Alvaro⁴²³,Zhang Xiaoyi⁵⁶²³,Tu Ming-Feng¹²³,Garrido-Barros Pablo⁷⁸⁹¹⁰,Mahy Jean-Pierre¹¹¹²¹³¹⁴¹⁵,Avenier Frédéric¹¹¹²¹³¹⁴¹⁵,Aukauloo Ally¹¹¹²¹³¹⁴¹⁵

Affiliation:

1. Chemical Sciences and Engineering Division

2. Lemont IL 60439

3. USA

4. Argonne Leadership Computing Facility

5. X-ray Science Division

6. Argonne National Laboratory

7. Institute of Chemical Research of Catalonia (ICIQ)

8. Avgda. Països Catalans

9. 43007 Tarragona

10. Spain

11. Institut de Chimie Moléculaire et des Matériaux d’Orsay (UMR CNRS 8182)

12. Bat 420

13. Rue Doyen G. Poitou

14. Université Paris-Sud

15. Orsay 91405

Abstract

Probing the light-induced two electron transfer processes at a diiron(iii,iii) multimolecular photocatalytic system.

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2017/CC/C6CC08748E

Reference28 articles.

1. Carboxylate as the Protonation Site in (Peroxo)diiron(III) Model Complexes of Soluble Methane Monooxygenase and Related Diiron Proteins

2. Dioxygen binding to diferrous centers. Models for diiron-oxo proteins

3. Models for diiron-oxo proteins: the peroxide adduct of Fe2(HPTB)(OH)(NO3)4

4. Catalytic oxygen activation versus autoxidation for industrial applications: a physicochemical approach

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