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Spectroscopic characterization of heme iron-nitrosyl species and their role in NO reductase mechanisms in diiron proteins
Pierre Moënne-Loccoz
Chemical Physiology and Biochemistry
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Contribution to journal
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Review article
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peer-review
92
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Dive into the research topics of 'Spectroscopic characterization of heme iron-nitrosyl species and their role in NO reductase mechanisms in diiron proteins'. Together they form a unique fingerprint.
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Medicine & Life Sciences
nitric-oxide reductase
100%
dinitrosyl iron complex
98%
Heme
61%
Nitric Oxide
45%
Proteins
20%
Archaea
15%
Electron Transport Complex IV
14%
copper oxidase
10%
Denitrification
10%
Flavoproteins
8%
Nitrosative Stress
8%
Anaerobic Bacteria
7%
Nitrates
6%
Infections
5%
Metals
5%
Iron
5%
Membrane Proteins
5%
Theoretical Models
5%
Hemoglobins
4%
Electrons
4%
Signal Transduction
4%
Poisons
4%
Bacteria
4%
Enzymes
3%
Chemical Compounds
Nitric Oxide
53%
Heme
51%
Protein
23%
Cytochrome
8%
Cope Reaction
6%
Denitrification
6%
Signalling Molecule
6%
Resistance
6%
Flavoprotein
6%
Hemoglobin
4%
Reduction
4%
Toxic
3%
Nitrate
3%
Transition Element
3%
Molecular Cluster
3%
Molecule
1%