- Human pathology

Home > A. Molecular pathology > hemoproteins


Wednesday 30 July 2008

Definition: A hemoprotein (or haemoprotein), or heme protein, is a metalloprotein containing a heme prosthetic group, either covalently or noncovalently bound to the protein itself.

The iron in the heme is capable of undergoing oxidation and reduction (usually to +2 and +3, though stabilized ferryl [Fe+4] compounds are well known in the peroxidases).

Hemoproteins have diverse biological functions including:

- oxygen transport

  • hemoglobin
  • hemocyanin
  • myoglobin
  • neuroglobin
  • cytoglobin
  • leghemoglobin

- catalysis

  • peroxidases
  • cytochrome c oxidase
  • ligninases

- active membrane transport

  • cytochromes

- electron transfer

  • cytochrome c
  • catalase

- Sensory

  • FixL (Oxygen sensor)
  • sGC (Nitric Oxide sensor)
  • CooA (CO sensor)


Hemoproteins have diverse biological functions including the transportation of diatomic gases, chemical catalysis, diatomic gas detection, and electron transfer. It has been speculated that the original evolutionary function of hemoproteins was electron transfer in primitive sulfur-based photosynthesis pathways in ancestral cyanobacteria before the appearance of molecular oxygen.

The heme iron serves as a source or sink of electrons during electron transfer or redox chemistry.

In peroxidase reactions, the porphyrin molecule also serves as an electron source.

In the transportation or detection of diatomic gases, the gas binds to the heme iron. During the detection of diatomic gases, the binding of the gas ligand to the heme iron induces conformational changes in the surrounding protein.

Hemoproteins achieve their remarkable functional diversity by modifying the environment of the heme macrocycle within the protein matrix.

For example, the ability of hemoglobin to effectively deliver oxygen to tissues is due to specific amino acid residues located near the heme molecule.

Bohr effect

Hemoglobin binds oxygen in the pulmonary vasculature, where the pH is high and the pCO2 is low, and releases it in the tissues, where the situations are reversed. This phenomenon is known as the Bohr effect.

The molecular mechanism behind this effect is the steric organization of the globin chain; a histidine residue, located adjacent to the heme group, becomes positively charged under acid circumstances, sterically releasing oxygen from the heme group.