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heme oxidation

Known as: haem oxidation 
The chemical reactions and pathways resulting in the loss of electrons from one or more atoms in heme. [GOC:mah]
National Institutes of Health

Papers overview

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Highly Cited
2009
Highly Cited
2009
Design and engineering of an O(2) transport protein
The principles of natural protein engineering are obscured by overlapping functions and complexity accumulated through natural… Expand
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Highly Cited
2003
Highly Cited
2003
How cytochromes with different folds control heme redox potentials.
The electrochemical midpoint potentials (E(m)'s) of 13 cytochromes, in globin (c, c(2), c(551), c(553)), four-helix bundle (c', b… Expand
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Highly Cited
1998
Highly Cited
1998
Evidence for Heme-mediated Redox Regulation of Human Cystathionine β-Synthase Activity*
Human cystathionine β-synthase catalyzes the first step in the catabolic removal of the toxic metabolite, homocysteine. It is… Expand
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Highly Cited
1997
Highly Cited
1997
The importance of the protein in controlling the electrochemistry of heme metalloproteins: methods of calculation and analysis
Abstract The importance of electrostatic effects in determining the free energy of redox reactions in proteins such as… Expand
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Highly Cited
1987
Highly Cited
1987
Dual control mechanism for heme oxygenase: tin(IV)-protoporphyrin potently inhibits enzyme activity while markedly increasing content of enzyme protein in liver.
Tin(IV)-protoporphyrin (Sn-protoporphyrin) potently inhibits heme degradation to bile pigments in vitro and in vivo, a property… Expand
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Highly Cited
1982
Highly Cited
1982
Purification and properties of bovine spleen heme oxygenase. Amino acid composition and sites of action of inhibitors of heme oxidation.
Microsomal heme oxygenase has been purified from bovine spleen to homogeneity using DEAE-cellulose chromatography, initial… Expand
Highly Cited
1981
Highly Cited
1981
Prevention of neonatal hyperbilirubinemia by tin protoporphyrin IX, a potent competitive inhibitor of heme oxidation.
The effects of various metalloporphyrins on hepatic heme oxygenase (EC 1.14.99.3) activity were examined in order to identify… Expand
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Highly Cited
1976
Highly Cited
1976
Studies on the mechanism of induction of haem oxygenase by cobalt and other metal ions.
Cobalt ions (Co2+) are potent inducers of haem oxygenase in liver and inhibit microsomal drug oxidation probably by depleting… Expand
Highly Cited
1975
Highly Cited
1975
Cobalt stimulation of heme degradation in the liver. Dissociation of microsomal oxidation of heme from cytochrome P-450.
The administration of cobalt to rats caused a marked increase in the oxidative degradation of heme (hematin, iron protoporphyrin… Expand
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Highly Cited
1974
Highly Cited
1974
Cobalt induction of hepatic heme oxygenase; with evidence that cytochrome P-450 is not essential for this enzyme activity.
  • M. Maines, A. Kappas
  • Proceedings of the National Academy of Sciences…
  • 1974
    • Corpus ID: 24805215
Treatment of rats in vivo with cobalt chloride stimulated heme oxidation by hepatic microsomes to levels up to 800% above… Expand
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