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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

Semantic Scholar uses AI to extract papers important to this topic.
Review
2016
Review
2016
BACH1, the master regulator gene: A novel candidate target for cancer therapy.
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… 
Review
2003
Review
2003
The heme oxygenase system: its role in liver inflammation.
Heme Oxygenase is the rate-limiting enzyme in the degradation of heme into carbon monoxide (CO), iron and bilirubin. To date… 
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… 
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… 
Review
1995
Review
1995
Nitric oxide (NO) protects against cellular damage by reactive oxygen species.
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… 
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… 
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… 
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. MainesA. Kappas
  • Proceedings of the National Academy of Sciences…
  • 1974
  • Corpus ID: 7998312
Treatment of rats in vivo with cobalt chloride stimulated heme oxidation by hepatic microsomes to levels up to 800% above… 
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