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ferryl iron
Known as:
iron iv
, iron(IV)
, iron (4+) ion
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National Institutes of Health
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1 relation
Broader (1)
Iron
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Review
2013
Review
2013
FENTON REACTION DRIVEN BY IRON LIGANDS
P. Salgado
,
Victoria Melin
,
D. Contreras
,
Y. Moreno
,
H. Mansilla
2013
Corpus ID: 97471052
ABSTRACT One of the most important sources of reactive oxygen species (ROS) in biological systems is the Fenton reaction. In this…
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Highly Cited
2010
Highly Cited
2010
Photodegradation of organic dyes in the presence of [Fe(III)-salen]Cl complex and H2O2 under visible light irradiation.
Sarifuddin Gazi
,
A. Rajakumar
,
N.D. Pradeep Singh
Journal of Hazardous Materials
2010
Corpus ID: 40949182
Highly Cited
2008
Highly Cited
2008
Ligand-enhanced reactive oxidant generation by nanoparticulate zero-valent iron and oxygen.
Christina R. Keenan
,
D. Sedlak
Environmental Science and Technology
2008
Corpus ID: 3069772
The reaction of zero-valent iron or ferrous iron with oxygen produces reactive oxidants capable of oxidizing organic compounds…
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Highly Cited
2007
Highly Cited
2007
Ferryl haem protonation gates peroxidatic reactivity in globins.
Radu Silaghi-Dumitrescu
,
B. Reeder
,
P. Nicholls
,
C. Cooper
,
Michael T. Wilson
Biochemical Journal
2007
Corpus ID: 44370039
Ferryl (Fe(IV)=O) species are involved in key enzymatic processes with direct biomedical relevance; among others, the…
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Review
2006
Review
2006
Structure and mechanism in the bacterial dihaem cytochrome c peroxidases.
G. Pettigrew
,
A. Echalier
,
S. R. Pauleta
Journal of Inorganic Biochemistry
2006
Corpus ID: 38672087
Highly Cited
2002
Highly Cited
2002
Kinetic Characterization of Compound I Formation in the Thermostable Cytochrome P450 CYP119*
David G. Kellner
,
S. Hung
,
K. Weiss
,
S. Sligar
Journal of Biological Chemistry
2002
Corpus ID: 6677918
The kinetics of formation and breakdown of the putative active oxygenating intermediate in cytochrome P450, a ferryl-oxo…
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Highly Cited
1996
Highly Cited
1996
Redox cycling of human methaemoglobin by H2O2 yields persistent ferryl iron and protein based radicals.
Rakesh P. Patel
,
D. Svistunenko
,
V. Darley-Usmar
,
Martyn C. R. Symons
,
Michael T. Wilson
Free radical research
1996
Corpus ID: 45035132
The formation and reactivity of ferryl haemoglobin (and myoglobin), which occurs on addition of H2O2, has been proposed as a…
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Highly Cited
1995
Highly Cited
1995
Reduction of ferrylmyoglobin and ferrylhemoglobin by nitric oxide: a protective mechanism against ferryl hemoprotein-induced oxidations.
N. Gorbunov
,
A. Osipov
,
B. Day
,
Beatriz Zayas-Rivera
,
V. Kagan
,
N. Elsayed
Biochemistry
1995
Corpus ID: 34241625
The reactions of metmyoglobin (metMb) and methemoglobin (metHb), oxidized to their respective oxoferryl free radical species (.Mb…
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Highly Cited
1987
Highly Cited
1987
Oxidation of oxymyoglobin to metmyoglobin with hydrogen peroxide: involvement of ferryl intermediate.
Keisuke Yusa
,
Shikama Keiji
Biochemistry
1987
Corpus ID: 42590668
Hydrogen peroxide, one of the potent oxidants in muscle tissues, can induce very rapid oxidation of oxymyoglobin (MbO2) to…
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Highly Cited
1985
Highly Cited
1985
Myoglobin-catalyzed hydrogen peroxide dependent arachidonic acid peroxidation.
M. B. Grisham
Journal of Free Radicals in Biology & Medicine
1985
Corpus ID: 20154125
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