Nature of haem-haem interaction.

Nature ·Vol. 237 ·No. 5357 ·1972-06-30 ·Pages 495-9

Perutz MF

Abstract

Haem-haem interaction consists of a change of tension at the haems, caused by a transition between two alternative quaternary structures of the protein. Dr Perutz describes how spin changes that accompany reaction with ligands alter the oxygen affinity of the haems.

MeSH Terms

Allosteric Regulation Allosteric Site Crystallography, X-Ray Heme/chemistry,metabolism Hemoglobins/chemistry,metabolism Humans Iron/chemistry,metabolism Oxygen/metabolism Protein Structure, Quaternary Spectroscopy, Near-Infrared Static Electricity Thermodynamics

Chemicals

Hemoglobins Heme Iron Oxygen

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Perutz M F

MRC Laboratory of Molecular Biology, Hills Road, Cambridge.

Article Info

Journal

Nature

Abbr.

Nature

ISSN

0028-0836

DOI

10.1038/237495a0

Published

1972-06-30

Pages

495-9

Language

English

Region

England

NLM ID

0410462

Subset

External Links

PubMed source DOI: 10.1038/237495a0 View journal details

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Nature of haem-haem interaction.

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