Explore: Hème

Heme (American English), or haem (Commonwealth English, both pronounced /hi:m/ HEEM), is a ring-shaped iron-containing molecule that commonly serves as

Heme A (or haem A) is a heme, a coordination complex consisting of a macrocyclic ligand called a porphyrin, chelating an iron atom. Heme A is a biomolecule

(about 20–25% of the total) as carbaminohemoglobin, in which CO2 binds to the heme protein. The molecule also carries the important regulatory molecule nitric

Heme B or haem B (also known as protoheme IX) is the most abundant heme. Hemoglobin and myoglobin are examples of oxygen transport proteins that contain

Heme oxygenase, or haem oxygenase, (HMOX, commonly abbreviated as HO) is an enzyme that catalyzes the degradation of heme to produce biliverdin, ferrous

haemoprotein), or heme protein, is a protein that contains a heme prosthetic group. They are a very large class of metalloproteins. The heme group confers

PolyHeme was a proposed temporary oxygen-carrying blood substitute made from human hemoglobin for emergency treatment of trauma situations where large

person's parents and are due to a mutation in one of the genes that make heme. They may be inherited in an autosomal dominant, autosomal recessive, or

A heme transporter is a protein that delivers heme to the various parts of a biological cell that require it. Heme is a major source of dietary iron in

Heme C (or haem C) is an important kind of heme. The correct structure of heme C was published in mid 20th century by the Swedish biochemist K.-G. Paul