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A Combined Far-Infrared Spectroscopic and Electrochemical Approach for the Study of Iron-Sulfur Proteins
scientific article published on 02 September 2011
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Europe PubMed Central
PubMed publication ID
21887734
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21887734%20AND%20SRC:MED&resulttype=core&format=json
retrieved
12 February 2020
title
A combined far-infrared spectroscopic and electrochemical approach for the study of iron-sulfur proteins
(English)
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Europe PubMed Central
PubMed publication ID
21887734
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21887734%20AND%20SRC:MED&resulttype=core&format=json
retrieved
12 February 2020
main subject
infrared spectroscopy
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author
Petra Hellwig
series ordinal
2
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Europe PubMed Central
PubMed publication ID
21887734
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21887734%20AND%20SRC:MED&resulttype=core&format=json
retrieved
12 February 2020
author name string
Youssef El Khoury
series ordinal
1
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Europe PubMed Central
PubMed publication ID
21887734
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21887734%20AND%20SRC:MED&resulttype=core&format=json
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12 February 2020
publication date
2 September 2011
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Europe PubMed Central
PubMed publication ID
21887734
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12 February 2020
published in
ChemPhysChem
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PubMed publication ID
21887734
reference URL
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12 February 2020
volume
12
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Europe PubMed Central
PubMed publication ID
21887734
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12 February 2020
issue
14
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Europe PubMed Central
PubMed publication ID
21887734
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12 February 2020
page(s)
2669-2674
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Europe PubMed Central
PubMed publication ID
21887734
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12 February 2020
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Redox Dependent Changes at the Heme Propionates in CytochromecOxidase fromParacoccusdenitrificans: Direct Evidence from FTIR Difference Spectroscopy in Combination with Heme Propionate13C Labeling†
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Electrochemically induced FTIR difference spectroscopy in the mid- to far infrared (200 μm) domain: A new setup for the analysis of metal–ligand interactions in redox proteins
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Low-frequency heme, iron-ligand, and ligand modes of imidazole and imidazolate complexes of iron protoporphyrin and microperoxidase in aqueous solution. An analysis by far-infrared difference spectroscopy
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EPR spectroscopic characterization of the iron-sulphur proteins and cytochrome P-450 in mitochondria from the insect Spodoptera littoralis (cotton leafworm).
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Complete Thermodynamic Characterization of Reduction and Protonation of thebc1-type Rieske [2Fe-2S] Center ofThermus thermophilus
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Characterization of the pH-dependent resonance Raman transitions of archaeal and bacterial Rieske [2Fe-2S] proteins.
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Resonance Raman characterization of archaeal and bacterial Rieske protein variants with modified hydrogen bond network around the [2Fe-2S] center.
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N-isotope effects on the Raman spectra of Fe(2)S(2) ferredoxin and Rieske ferredoxin: evidence for structural rigidity of metal sites
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Normal mode analysis of Pyrococcus furiosus rubredoxin via nuclear resonance vibrational spectroscopy (NRVS) and resonance raman spectroscopy
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Dynamics of Rhodobacter capsulatus [2FE-2S] ferredoxin VI and Aquifex aeolicus ferredoxin 5 via nuclear resonance vibrational spectroscopy (NRVS) and resonance Raman spectroscopy.
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The Environment of [2Fe-2S] Clusters in Ferredoxins: The Role of Residue 45 Probed by Site-Directed Mutagenesis
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Probing the hydrogen bonding structure in the Rieske protein
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Direct observation of redox-linked histidine protonation changes in the iron-sulfur protein of the cytochrome bc1 complex by ATR-FTIR spectroscopy
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Spectroscopic characterization of site-specific [Fe(4)S(4)] cluster chemistry in ferredoxin:thioredoxin reductase: implications for the catalytic mechanism.
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Structure of a water soluble fragment of the 'Rieske' iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 A resolution
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Atomic Resolution Structures of Rieske Iron-Sulfur Protein: Role of Hydrogen Bonds in Tuning the Redox Potential of Iron-Sulfur Clusters
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High-resolution structure of the soluble, respiratory-type Rieske protein from Thermus thermophilus: analysis and comparison
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Mutational analysis of residues forming hydrogen bonds in the Rieske [2Fe-2S] cluster of the cytochrome bc1 complex in Paracoccus denitrificans
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Alteration of the midpoint potential and catalytic activity of the rieske iron-sulfur protein by changes of amino acids forming hydrogen bonds to the iron-sulfur cluster
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Negatively charged residues and hydrogen bonds tune the ligand histidine pKa values of Rieske iron-sulfur proteins
1 reference
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Proton environment of reduced Rieske iron-sulfur cluster probed by two-dimensional ESEEM spectroscopy.
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Identification of Hydrogen Bonds to the Rieske Cluster through the Weakly Coupled Nitrogens Detected by Electron Spin Echo Envelope Modulation Spectroscopy
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Identifiers
DOI
10.1002/CPHC.201100165
1 reference
stated in
Europe PubMed Central
PubMed publication ID
21887734
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21887734%20AND%20SRC:MED&resulttype=core&format=json
retrieved
12 February 2020
PubMed publication ID
21887734
1 reference
stated in
Europe PubMed Central
PubMed publication ID
21887734
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21887734%20AND%20SRC:MED&resulttype=core&format=json
retrieved
12 February 2020
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