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Heme

Known as: Haem, ferroheme, Reduced Hematin 
The part of certain molecules that contains iron. The heme part of hemoglobin is the substance inside red blood cells that binds to oxygen in the… 
National Institutes of Health

Papers overview

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Highly Cited
1986
Highly Cited
1986
A soluble high affinity binding unit for leukotriene (LT) C4 in the high speed supernatant of rat liver homogenate was… 
Highly Cited
1986
Highly Cited
1984
Highly Cited
1984
Soret excitation of canine myeloperoxidase (MPO) gives rise to a complex resonance Raman (RR) spectrum characterized by multiple… 
Highly Cited
1977
Highly Cited
1977
1. Qualitative and quantitative studies of the porphyrins and the porphyrinogen carboxylyase of the liver, spleen, kidney… 
Highly Cited
1974
Highly Cited
1974
Bakers' yeast cytochrome b2 [lL-(+)-lactate dehydrogenase or l-(+)-lactate cytochrome c oxidoreductase], usually purified by… 
Highly Cited
1971
Highly Cited
1971
The atomic structure of the monomeric insect haemoglobin is closely similar to the structure of whale myoglobin, although only… 
Review
1970
Review
1970
  • G. Lang
  • 1970
  • Corpus ID: 30474496
A fair beginning has been made in understanding the Mössbauer spectra of many types of haem proteins. The diamagnetic compounds… 
Highly Cited
1970
Highly Cited
1970
THE alkaline Bohr effect is the uptake of protons at a pH greater than 6 when oxygen is removed from haemoglobin1. In horse… 
Highly Cited
1970
Highly Cited
1967
Highly Cited
1967
1. The preparation and characterization of manganese, iron, cobalt, nickel, copper and zinc metalloporphyrins is described…