Articles citing this article

The Citing articles tool gives a list of articles citing the current article.
The citing articles come from EDP Sciences database, as well as other publishers participating in CrossRef Cited-by Linking Program. You can set up your personal account to receive an email alert each time this article is cited by a new article (see the menu on the right-hand side of the abstract page).

Cited article:

Electronic Structure of Tetrahedral,S= 2, [Fe{(EPiPr2)2N}2], E = S, Se, Complexes: Investigation by High-Frequency and -Field Electron Paramagnetic Resonance,57Fe Mössbauer Spectroscopy, and Quantum Chemical Studies

Sebastian A. Stoian, Mahsa Moshari, Eleftherios Ferentinos, et al.
Inorganic Chemistry 60 (15) 10990 (2021)
https://doi.org/10.1021/acs.inorgchem.1c00670

Spontaneous assembly of redox-active iron-sulfur clusters at low concentrations of cysteine

Sean F. Jordan, Ioannis Ioannou, Hanadi Rammu, et al.
Nature Communications 12 (1) (2021)
https://doi.org/10.1038/s41467-021-26158-2

Rubredoxins derivatives: Simple sulphur-rich coordination metal sites and its relevance for biology and chemistry

Biplab K. Maiti, Rui M. Almeida, Isabel Moura and José J.G. Moura
Coordination Chemistry Reviews 352 379 (2017)
https://doi.org/10.1016/j.ccr.2017.10.001

Mössbauer spectroscopy of Fe/S proteins

Maria-Eirini Pandelia, Nicholas D. Lanz, Squire J. Booker and Carsten Krebs
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1853 (6) 1395 (2015)
https://doi.org/10.1016/j.bbamcr.2014.12.005

Modeling the Active Site of [NiFe] Hydrogenases and the [NiFeu] Subsite of the C-Cluster of Carbon Monoxide Dehydrogenases: Low-Spin Iron(II) Versus High-Spin Iron(II)

Katharina Weber, Özlen F. Erdem, Eckhard Bill, Thomas Weyhermüller and Wolfgang Lubitz
Inorganic Chemistry 53 (12) 6329 (2014)
https://doi.org/10.1021/ic500910z

Spectroscopic and Functional Characterization of Iron-Bound Forms of Azotobacter vinelandiiNifIscA

Daphne T. Mapolelo, Bo Zhang, Sunil G. Naik, Boi Hanh Huynh and Michael K. Johnson
Biochemistry 51 (41) 8056 (2012)
https://doi.org/10.1021/bi300664j

Monooxygenase‐Like Reactivity of an Unprecedented Heterobimetallic {FeO2Ni} Moiety

Shenglai Yao, Christian Herwig, Yun Xiong, et al.
Angewandte Chemie International Edition 49 (39) 7054 (2010)
https://doi.org/10.1002/anie.201001914

Monooxygenase‐Like Reactivity of an Unprecedented Heterobimetallic {FeO2Ni} Moiety

Shenglai Yao, Christian Herwig, Yun Xiong, et al.
Angewandte Chemie 122 (39) 7208 (2010)
https://doi.org/10.1002/ange.201001914

Spectroscopic evidence for an all-ferrous [4Fe–4S]0 cluster in the superreduced activator of 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans

Marcus Hans, Wolfgang Buckel and Eckhard Bill
JBIC Journal of Biological Inorganic Chemistry 13 (4) 563 (2008)
https://doi.org/10.1007/s00775-008-0345-z

Studies of Iron‐Sulfur Covalency in the Model System and Proteins

Xiu‐Juan Qin, Yan Chen and Fa‐Ming Gao
Chinese Journal of Chemistry 23 (9) 1203 (2005)
https://doi.org/10.1002/cjoc.200591203

Magnetic and optical anisotropy of Clostridium pasteurianum rubredoxin from optically detected electron paramagnetic resonance

Birgit Börger and Dieter Suter
The Journal of Chemical Physics 115 (21) 9821 (2001)
https://doi.org/10.1063/1.1415461

Inadequacies of the Point-Dipole Approximation for Describing Electron−Nuclear Interactions in Paramagnetic Proteins:  Hybrid Density Functional Calculations and the Analysis of NMR Relaxation of High-Spin Iron(III) Rubredoxin

Steven J. Wilkens, Bin Xia, Brian F. Volkman, et al.
The Journal of Physical Chemistry B 102 (42) 8300 (1998)
https://doi.org/10.1021/jp982018q

Induced paramagnetism and hyperfine interactions in the {[Fe4S4]-Fe} active site of Escherichia coli sulfite reductase

Moisey I. Belinsky
Chemical Physics Letters 250 (3-4) 320 (1996)
https://doi.org/10.1016/0009-2614(95)01456-X

A Serine → Cysteine Ligand Mutation in the High Potential Iron−Sulfur Protein from Chromatium vinosum Provides Insight into the Electronic Structure of the [4Fe−4S] Cluster

Elena Babini, Ivano Bertini, Marco Borsari, et al.
Journal of the American Chemical Society 118 (1) 75 (1996)
https://doi.org/10.1021/ja952636+

Characterization of the Iron-binding Site in Mammalian Ferrochelatase by Kinetic and Mössbauer Methods

Ricardo Franco, José J.G. Moura, Isabel Moura, et al.
Journal of Biological Chemistry 270 (44) 26352 (1995)
https://doi.org/10.1074/jbc.270.44.26352

Mammalian ferrochelatase, a new addition to the metalloenzyme family.

G.C. Ferreira, R. Franco, S.G. Lloyd, A.S. Pereira, I. Moura, J.J. Moura and B.H. Huynh
Journal of Biological Chemistry 269 (10) 7062 (1994)
https://doi.org/10.1016/S0021-9258(17)37245-9

Mössbauer studies on yeast metallothionein

X. -Q. Ding, E. Bill, A. X. Trautwein, H. J. Hartmann and U. Weser
Hyperfine Interactions 91 (1) 791 (1994)
https://doi.org/10.1007/BF02064608

Mössbauer and magnetic susceptibility studies on iron(II) metallothionein from rabbit liver

Xiao‐Qi DING, Christian BUTZLAFF, Eckhard BILL, et al.
European Journal of Biochemistry 220 (3) 827 (1994)
https://doi.org/10.1111/j.1432-1033.1994.tb18685.x

Heisenberg model for tetrameric iron clusters in high-potential iron-sulfur proteins. II. Double exchange in distorted cluster

M. Belinskii
Chemical Physics 176 (1) 37 (1993)
https://doi.org/10.1016/0301-0104(93)85005-S

Heisenberg model for tetrameric iron clusters in high-potential iron-sulfur proteins. I. Exchange states, g-factors, hyperfine interactions

M. Belinskii
Chemical Physics 176 (1) 15 (1993)
https://doi.org/10.1016/0301-0104(93)85004-R

Static and dynamic hyperfine coupling of FE(II) in the FeS4 unit. Results of Mössbauer spectroscopy on a [P(C6H5)4]2[Fe(SC6H5)4] monocrystal

H. Winkler, E. Bill, A. X. Trautwein, et al.
The Journal of Chemical Physics 89 (2) 732 (1988)
https://doi.org/10.1063/1.455196

Mössbauer studies on the metal‐thiolate cluster formation in Fe(II)‐metallothionein

Xiaoqi DING, Eckhard BILL, Meinrad GOOD, Alfred X. TRAUTWEIN and Milan VAŠÁK
European Journal of Biochemistry 171 (3) 711 (1988)
https://doi.org/10.1111/j.1432-1033.1988.tb13843.x

Spin fluctuations of paramagnetic iron centers in proteins and model complexes: Mössbauer and EPR results

C. E. Schulz, P. Nyman and P. G. Debrunner
The Journal of Chemical Physics 87 (9) 5077 (1987)
https://doi.org/10.1063/1.453675

Structure and magnetism of iron-sulfur clusters in proteins

Eckard Münck and Thomas A. Kent
Hyperfine Interactions 27 (1-4) 161 (1986)
https://doi.org/10.1007/BF02354752

Iron sulfur and iron molybdenum sulfur compounds: Comparison of molecular orbital calculations and spin‐Hamiltonian analysis of Mössbauer spectra

A. X. Trautwein, E. Bill, R. Bläs, et al.
The Journal of Chemical Physics 82 (8) 3584 (1985)
https://doi.org/10.1063/1.448916

Mössbauer investigation of the cofactor iron of putidamonooxin

Eckhard BILL, Frithjof‐Hans BERNHARDT, Alfred Xaver TRAUTWEIN and Heiner WINKLER
European Journal of Biochemistry 147 (1) 177 (1985)
https://doi.org/10.1111/j.1432-1033.1985.tb08734.x

Mössbauer Studies on the Active Fe …[2Fe‐2S] Site of Putidamonooxin, Its Electron Transport and Dioxygen Activation Mechanism

Eckhard BILL, Frithjof‐Hans BERNHARDT and Alfred Xaver TRAUTWEIN
European Journal of Biochemistry 121 (1) 39 (1981)
https://doi.org/10.1111/j.1432-1033.1981.tb06426.x

Evidence for a three-iron center in a ferredoxin from Desulfovibrio gigas. Mössbauer and EPR studies.

B.H. Huynh, J.J. Moura, I. Moura, T.A. Kent, J. LeGall, A.V. Xavier and E. Münck
Journal of Biological Chemistry 255 (8) 3242 (1980)
https://doi.org/10.1016/S0021-9258(19)85685-5

Interpretation of the Mossbauer Spectra of the Four-Iron Ferredoxin from Bacillus stearothermophilus

Peter MIDDLETON, Dominic P. E. DICKSON, Charles E. JOHNSON and James D. RUSH
European Journal of Biochemistry 88 (1) 135 (1978)
https://doi.org/10.1111/j.1432-1033.1978.tb12430.x

High‐field Mössbauer studies of reduced protocatechuate 3,4‐dioxygenase

R. Zimmermann, B. H. Huynh, E. Münck and J. D. Lipscomb
The Journal of Chemical Physics 69 (12) 5463 (1978)
https://doi.org/10.1063/1.436538