Max Ferdinand Perutz | Hemoglobin molecular structure determiner

Max Ferdinand Perutz – determined hemoglobin structure

Article on Max Ferdinand Perutz

Biography & contributions

Max Ferdinand Perutz was Austrian-born British biochemist and Nobel laureate born on May 19, 1914 – died on February 06, 2002. Perutz received many notable awards and prizes in his life time which includes 1962 Perutz received Nobel Prize, in the year of 1971 he got Royal Medal, in the year of 1979 Perutz Copley Medal.

His important biochemistry related works include in the year of 1953 Perutz showed that diffracted X-rays from protein crystals could be phased by comparing the patterns from crystals of the protein with and without heavy atoms attached, in the year of 1959 he determined molecular structure of hemoglobin, myoglobin and he employed this method to determine the molecular structure of the protein hemoglobin, which transports oxygen in the blood.


Hemoglobin is an iron-containing protein in the blood of many animals. It develops in cells in the bone marrow that become red blood cells. Each hemoglobin molecule is made up of four heme groups surrounding a globin group, forming a tetrahedral structure. Heme, which accounts for only 4 percent of the weight of the molecule, is composed of a ringlike organic compound known as a porphyrin to which an iron atom is attached. It is the iron atom that binds oxygen as the blood travels between the lungs and the tissues. There are four iron atoms in each molecule of hemoglobin, which accordingly can bind four atoms of oxygen. Globin consists of two linked pairs of polypeptide chains.

Hemoglobin is involved in the transport of other gases: It carries some of the body's respiratory carbon dioxide (about 10% of the total) as carbaminohemoglobin, in which CO2 is bound to the globin protein.

Hemoglobin and hemoglobin-like molecules are also found in many invertebrates, fungi, and plants. In these organisms, hemoglobins may carry oxygen, or they may act to transport and regulate other things such as carbon dioxide, nitric oxide, hydrogen sulfide and sulfide. Besides the oxygen ligand, which binds to hemoglobin in a cooperative manner, hemoglobin ligands also include competitive inhibitors such as carbon monoxide (CO) and allosteric ligands such as carbon dioxide (CO2) and nitric oxide (NO). Hemoglobin also has competitive binding affinity for cyanide (CN), sulfur monoxide (SO) and sulfide (S2−), including hydrogen sulfide (H2S). Hemoglobin also carries nitric oxide in the globin part of the molecule. This improves oxygen delivery in the periphery and contributes to the control of respiration.

A variant of the molecule, called leghemoglobin, is used to scavenge oxygen away from anaerobic systems, such as the nitrogen-fixing nodules of leguminous plants, before the oxygen can poison the system.

Hemoglobin has a quaternary structure characteristic of many multi-subunit globular proteins. Hemoglobin's quaternary structure comes from its four subunits in roughly a tetrahedral arrangement. 

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