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Max Perutz revealed the structure of haemoglobin

In 1959, 22 years after he began, Max Perutz determined the structure of haemoglobin, the blood's oxygen carrier, sharing the 1962 Nobel Prize in Chemistry.

Max Perutz
Max Perutz · 1914–2002
Person
Max Perutz
Lived
1914–2002
Field
Molecular biology
From
Austrian-British

The story

Haemoglobin is the protein in red blood cells that carries oxygen from the lungs to the rest of the body. In September 1937 Max Perutz, a young research student from Vienna working at the Cavendish Laboratory in Cambridge, learned from his cousin Felix Haurowitz in Prague that the oxygen-carrying and oxygen-free forms of haemoglobin form different crystals. He decided to work out its three-dimensional structure and so solve a great problem in biochemistry. No one had ever determined the structure of anything nearly so large: haemoglobin has a molecular weight of about 64,500.

The work spanned two worlds. The biochemist G. S. Adair made him his first crystals of horse haemoglobin, the protein chemistry was done at David Keilin's Molteno Institute and the X-ray work at the Cavendish, with Perutz bridging the gap between biology and physics on his bicycle. He completed his PhD in 1940, but his early attempts to calculate the structure led to misleading results.

His 1953 discovery that heavy atoms such as mercury could be attached to the protein without disturbing its crystals finally made the problem solvable. A full three-dimensional picture needed several different heavy-atom derivatives, and it took years more of work. In 1959 Perutz and his colleagues produced the first three-dimensional model of haemoglobin, showing its four protein chains, the coils of alpha helix within them and their iron-containing haem groups. It closely resembled myoglobin, which his colleague John Kendrew had solved by similar methods, and when the amino acid sequences became available they fitted the structures well.

In 1962 Perutz shared the Nobel Prize in Chemistry with Kendrew for their studies of the structures of globular proteins. Haemoglobin and myoglobin were the first proteins whose shapes anyone had seen. Through the 1960s Perutz's team refined the structures of both forms of haemoglobin to atomic detail, which allowed him to explain how the molecule picks up and releases oxygen.

The achievement proved that the molecules of life could be mapped atom by atom. It opened the way to structural biology, now used to understand how proteins work, how mutations cause disease and how new medicines can be designed to fit their targets.

Why it matters

Seeing haemoglobin's structure proved that the molecules of life could be mapped atom by atom, opening the way to understanding thousands of proteins.

About Max Perutz

Viennese refugee who spent 22 years solving the structure of haemoglobin, won the 1962 Nobel Prize and built the Cambridge laboratory where molecular biology came of age.

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Max Perutz
1914–2002 · Molecular biology
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Sources

Another act of tikkun olam. This is part of tikkun olam, the Jewish idea of repairing the world, and every one of us can add to it.

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