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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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2012
2012
Heme-assisted S-Nitrosation Desensitizes Ferric Soluble Guanylate Cyclase to Nitric Oxide*
Background: Oxidation of the sGC heme iron causes dysfunction in NO/cGMP signal transduction, a key pathway in cardiovascular… 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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1998
1998
Peroxynitrite-mediated heme oxidation and protein modification of native and chemically modified hemoglobins.
Peroxynitrite (ONOO-) has been shown to play a critical role in tissue reperfusion injury. We have studied the reactions of ONOO… Expand
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Review
1995
Review
1995
Nitric oxide (NO) protects against cellular damage by reactive oxygen species.
Since the discovery of nitric oxide (NO) as an endogenously formed radical, its effect on numerous physiological processes has… 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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1982
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
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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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1975
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.
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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