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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

Related topics

Related topics

39 relations

Narrower (27)

2,4-dibromodeuteroheme2,4-dimethyldeuteroheme2-formyl-4-vinylhemeFerrihaem
HeminIron Compounds, OrganicProcess of secretionagonists

Broader (2)

Iron Compounds, UnspecifiedMetalloporphyrins

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
1987
Highly Cited
1987
Cytochrome P-450 and synthetic models
Abstract 
Highly Cited
1984
Highly Cited
1984
Structural analysis of myeloperoxidase by resonance Raman spectroscopy.
Soret excitation of canine myeloperoxidase (MPO) gives rise to a complex resonance Raman (RR) spectrum characterized by multiple… 
Highly Cited
1982
Highly Cited
1982
Evidence for hydrogen bonding of bound dioxygen to the distal histidine of oxycobalt myoglobin and haemoglobin
The origin of the differences in oxygen binding energy in various haemoglobins and myoglobins has long been debated. Perutz1… 
Highly Cited
1977
Highly Cited
1977
Porphyrins and porphyrinogen carboxy-lase in hexachlorobenzene-induced porphyria.
1. Qualitative and quantitative studies of the porphyrins and the porphyrinogen carboxylyase of the liver, spleen, kidney… 
Highly Cited
1974
Highly Cited
1974
Cytochrome b2 from bakers' yeast (L-lactate dehydrogenase). A double-headed enzyme.
Bakers' yeast cytochrome b2 [lL-(+)-lactate dehydrogenase or l-(+)-lactate cytochrome c oxidoreductase], usually purified by… 
Highly Cited
1973
Highly Cited
1973
Cellular Location and Concentration of Leghaemoglobin in Soybean Root Nodules
The reaction of leghaemoglobin (Lb) with oxidized 3,3'-diaminobenzidine has been used to demonstrate the localization of this… 
Highly Cited
1971
Highly Cited
1971
The atomic structure of erythrocruorin in the light of the chemical sequence and its comparison with myoglobin.
The atomic structure of the monomeric insect haemoglobin is closely similar to the structure of whale myoglobin, although only… 
Review
1970
Review
1970
Mössbauer spectroscopy of haem proteins
  • G. Lang
  • Quarterly Reviews of Biophysics (print)
  • 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
Inhibition of Bohr Effect after Removal of C-Terminal Histidines from Haemoglobin β-Chains
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
1967
Highly Cited
1967
Immunochemistry of sperm-whale myoglobins prepared with various modified porphyrins and metalloporphyrins.
1. The preparation and characterization of manganese, iron, cobalt, nickel, copper and zinc metalloporphyrins is described… 
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