English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Molybdenum L‐Edge XAS Spectra of MoFe Nitrogenase

Bjornsson, R., Delgado-Jaime, M. U., Lima, F. A., Sippel, D., Schlesier, J., Weyhermüller, T., et al. (2015). Molybdenum L‐Edge XAS Spectra of MoFe Nitrogenase. Zeitschrift für anorganische und allgemeine Chemie, 641(1), 65-71. doi:10.1002/zaac.201400446.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Bjornsson, Ragnar1, Author           
Delgado-Jaime, Mario U.1, Author           
Lima, Frederico A.1, Author           
Sippel, Daniel2, Author
Schlesier, Julia2, Author
Weyhermüller, Thomas1, Author           
Einsle, Oliver2, Author
Neese, Frank1, Author           
DeBeer, Serena1, Author           
Affiliations:
1Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society, ou_3023886              
2Institute for Biochemistry, Albert‐Ludwigs‐Universität Freiburg, Albertstrasse 21, 79104 Freiburg, Germany, ou_persistent22              

Content

show
hide
Free keywords: Nitrogenase; X-ray spectroscopy; L-edges; Molybdenum; FeMoco
 Abstract: A molybdenum L‐edge X‐ray absorption spectroscopy (XAS) study is presented for native and oxidized MoFe protein of nitrogenase as well as Mo‐Fe model compounds. Recently collected data on MoFe protein (in oxidized and reduced forms) is compared to previously published Mo XAS data on the isolated FeMo cofactor in NMF solution and put in context of the recent Mo K‐edge XAS study, which showed a MoIII assignment for the molybdenum atom in FeMoco. The L3‐edge data are interpreted within a simple ligand‐field model, from which a time‐dependent density functional theory (TDDFT) approach is proposed as a way to provide further insights into the analysis of the molybdenum L3‐edges. The calculated results reproduce well the relative spectral trends that are observed experimentally. Ultimately, these results give further support for the MoIII assignment in protein‐bound FeMoco, as well as isolated FeMoco.

Details

show
hide
Language(s): eng - English
 Dates: 2014-11-272015-01-01
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/zaac.201400446
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Zeitschrift für anorganische und allgemeine Chemie
  Abbreviation : Z. Anorg. Allg. Chem.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Leipzig, Weinheim : Verlag Johann Ambrosius Barth / Wiley-VCH
Pages: - Volume / Issue: 641 (1) Sequence Number: - Start / End Page: 65 - 71 Identifier: Other: 1521-3749
ISSN: 0044-2313
CoNE: https://pure.mpg.de/cone/journals/resource/954925453895