Showing papers by "Max F. Perutz published in 1971"
TL;DR: The atomic model of oxyhaemoglobin showed that the haemoglobin molecule is insensitive to replacements of most amino-acid residues on its surface but extremely sensitive to quite small alterations of internal non-polar contacts.
Abstract: WHEN the atomic model of oxyhaemoglobin had just been completed, we showed that the haemoglobin molecule is insensitive to replacements of most amino-acid residues on its surface but extremely sensitive to quite small alterations of internal non-polar contacts. And replacements near the haems and at the contacts between α and β subunits affect the respiratory function1.
127 citations
TL;DR: An X-ray crystallographic study of deoxyhaemoglobin Hiroshima has revealed that the replacement occurs not in position 143 but 146β, which supports the role of histidine 146β in the alkaline Bohr effect.
Abstract: HAEMOGLOBIN Hiroshima is a variant with interesting physiological properties1,2 discovered in a Japanese family. Its Bohr effect is halved, its oxygen affinity at physiological pH increased about three-fold, and haem-haem interaction is somewhat reduced compared with normal haemoglobin. In 0.1 M NaCl solutions initially stripped of phosphate, 2,3-diphospho-glycerate (2,3-DPG) diminishes the oxygen affinity as in haemoglobin A (H. F. Bunn, unpublished results). The amino-acid substitution originally deduced for this abnormal haemoglobin was histidine 143 (H21)β ⇐ aspartic acid1. It was possible to conceive of a mechanism which accounted for its diminished Bohr effect3, but the normal response of its oxygen affinity to 2,3-DPG was inconsistent with the proposed role of histidine 143 in 2,3-DPG binding by haemoglobin A4,5. An X-ray crystallographic study of deoxyhaemoglobin Hiroshima has now revealed that the replacement occurs not in position 143 but 146β. This was confirmed by chemical methods, and the physiological properties of this haemoglobin are now satisfactorily accounted for. The results support the role of histidine 146β in the alkaline Bohr effect6.
64 citations
TL;DR: The difference electron density map of deoxyhaemoglobin Rainier shows that the cysteine introduced by the mutation forms a disulphide bridge with the reactive cysteined, F9(93)β, of the same β-chain, thereby inhibiting part of the alkaline Bohr effect and haem–haem interaction.
Abstract: The difference electron density map of deoxyhaemoglobin Rainier (α2β2145Tyr→Cys) shows that the cysteine introduced by the mutation forms a disulphide bridge with the reactive cysteine, F9(93)β, of the same β-chain. The resulting structural distortions affect the C-terminus of the β-chain, thereby inhibiting part of the alkaline Bohr effect and haem–haem interaction.
40 citations
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TL;DR: An extract from the obituary for Sir Lawrence Bragg by M. F. Perutz [Nature (London), (1971), 233, 74, 74 and 76] can be found in this article.
Abstract: An extract from the obituary for Sir Lawrence Bragg by M. F. Perutz [Nature (London), (1971), 233, 74–76].
16 citations