Structure of Hæmoglobin: A Three-Dimensional Fourier Synthesis at 5.5-Å. Resolution, Obtained by X-Ray Analysis

Perutz, M. F.; Rossmann, Michael G.; Cullis, Ann F.; Muirhead, H.; Will, G.; North, A. C. T.

doi:10.1038/185416a0

Cited by 1,228 publications

(545 citation statements)

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“…As regards the arguments in favour of the first possibility, let us recall the dimple present on the molecular surface in the model put forward by Perutz el al. (5). If such a molecule is shadowed at a very low angle, as in the present case, in the direction shown in Fig.…”

Section: Resultsmentioning

confidence: 86%

“…The scattering curve of Rothwell (4) corresponds to an ellipsoidal molecule of dimensions 56 X 56 X 84 A. Very recently Perutz et al (5) considered this problem again and obtained a revised model of the molecule. In this model, the molecule looks like an ellipsoid of dimensions 64 X 55 X 50 A but has a dimple on the surface in the central region and a hole passing right through the molecule.…”

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confidence: 99%

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Electron Microscope Studies on the Haemoglobin Molecules

Chatterjee

Sadhukhan

Chatterjea

1961

The Journal of Cell Biology

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Haemoglobin molecules isolated from normal human subjects have been directly micrographed under the electron microscope following in general Hall's technique. The average height (h) and the widths along (wn) and perpendicular (wx) to the shadow direction of the molecules have been measured as 56.5 -4-6.6 A, 122.7 -4-15 A, and 120.9 ± 20 A, respectively. The exaggeration in the molecular widths due to the deposition of metal cap ranges between 60 to 70 A. The probable resolution of the substructure of the molecule, e.g., presence of "holes" and dimples, in the present electron microscopic evidence has been discussed. The electron microscopic results on the size of the individual haemoglobin molecules are in satisfactory agreement with the recent x-ray diffraction model of Perutz and his associates for horse haemoglobin.The haemoglobin molecule, the carrier of oxygen in blood, has been studied extensively by different authors. Its molecular weight is known very accurately (mol. wt. = 66,700) and the molecular structure has been determined from the x-ray diffraction studies of Bragg, Perutz, and their associates (1). According to these authors, the haemoglobin molecule is ellipsoidal in shape and has dimensions of 53 X 53 > 71 A in the hydrated condition and 45 X 45 X 65 A in the dry condition. Small angle x-ray scattering data are, however, not in very good agreement with the above model. Fournet (2) obtained a radius of gyration, R = 23 A, for horse haemoglobin. The radius of gyration corresponding to the x-ray diffraction model of dry haemoglobin molecule is 20 A and the axial ratio is 1.4. X-ray scattering data of Ritland, Kaesberg, and Beeman (3) and Rothwell (4) give an axial ratio of 1.5. The scattering curve of Rothwell (4) corresponds to an ellipsoidal molecule of dimensions 56 X 56 X 84 A. Very recently Perutz et al. (5) considered this problem again and obtained a revised model of the molecule. In this model, the molecule looks like an ellipsoid of dimensions 64 X 55 X 50 A but has a dimple on the surface in the central region and a hole passing right through the molecule. In the present work, attempts have been made to micrograph these molecules directly under the electron microscope, measure the dimensions, and find their agreement with the indirect physicochemical data. MATERIALS AND METHODSOxalated red blood cells, collected by venipuncturc from normal human subjects, were washed with cold isotonic saline four times and then hemolysed with twice their volume of distilled water and 0.4 volume of toluene. The hemolysed cells were spun down at 1,000 g for 30 minutes and the clear haemoglobin solution was pipettcd off. For further clarification, the haemoglobin solution thus obtained was centrifuged at 10,000 g for 15 minutes.The specimens for electron microscopic studies were prepared in general according to Hall's method (6). The purified human haemoglobin solution so obtained was dissolved in a buffer containing 0.05 M ammonium carbonate and O. 1 M ammonium ace-113 on

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Section: Resultsmentioning

confidence: 86%

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confidence: 99%

Electron Microscope Studies on the Haemoglobin Molecules

Chatterjee

Sadhukhan

Chatterjea

1961

The Journal of Cell Biology

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“…Dorothy Hodgkin went on to Oxford and determined structures of biologically important small molecules as well as proteins, most notably insulin [3,4]. Max Perutz arrived in Cambridge from Austria in 1936 and began his study of hemoglobin which led to its structure determination in 1959 [5]. Both Hodgkin and Perutz trained large numbers of crystallographers who set up laboratories around the world.…”

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confidence: 99%

The Protein Data Bank archive as an open data resource

Berman

Kleywegt

Nakamura

et al. 2014

J Comput Aided Mol Des

119

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“…In this respect, works by Adair (1) and Wyman (2,3) paved the way to a field of investigation which became explosive when Perutz and Kendrew solved for the first time the three-dimensional structure of myoglobin (Mb) (4) and hemoglobin (Hb) (5).…”

Section: Introductionmentioning

confidence: 99%

Multiple strategies for O2 transport: from simplicity to complexity

et al. 2007

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SummaryO 2 carriers (extracellular and intracellular as well as monomeric and multimeric) have evolved over the last billion of years, displaying iron and copper reactive centers; very different O 2 carriers may coexist in the same organism. Circulating O 2 carriers, faced to the external environment, are responsible for maintaining an adequate delivery of O 2 to tissues and organs almost independently of the environmental O 2 partial pressure. Then, intracellular globins facilitate O 2 transfer to mitochondria sustaining cellular respiration. Here, molecular aspects of multiple strategies evolved for O 2 transport and delivery are examined, from the simplest myoglobin to the most complex giant O 2 carriers and the red blood cell, mostly focusing on the aspects which have been mainly addressed by the so called 'Rome Group'.

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Structure of Hæmoglobin: A Three-Dimensional Fourier Synthesis at 5.5-Å. Resolution, Obtained by X-Ray Analysis

Cited by 1,228 publications

References 16 publications

Electron Microscope Studies on the Haemoglobin Molecules

Electron Microscope Studies on the Haemoglobin Molecules

The Protein Data Bank archive as an open data resource

Multiple strategies for O2 transport: from simplicity to complexity

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