Structure and function of haemoglobin

Muirhead, H.; Cox, Joyce M.; Mazzarella, L.; Perutz, M. F.

doi:10.1016/s0022-2836(67)80082-2

Cited by 282 publications

(67 citation statements)

References 14 publications

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“…(1978) tates essentially as a rigid body by 120 relative to the rest of the molecule, causing movements of as much as 8 A in the polypeptide backbone. This conformational change is comparable in both nature and magnitude to the change in quaternary structure seen in the allosteric transition of hemoglobin, in which the two ag dimers rotate 14°relative to one another as rigid units (21,25). Intrasubunit flexibility involving entire domains has also been observed in tomato bushy stunt virus coat protein (26) and in immunoglobulins (27).…”

Section: Discussionmentioning

confidence: 65%

Glucose-induced conformational change in yeast hexokinase.

Bennett¹,

Steitz²

1978

Proc. Natl. Acad. Sci. U.S.A.

299

127

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Section: Discussionmentioning

confidence: 65%

Glucose-induced conformational change in yeast hexokinase.

Bennett¹,

Steitz²

1978

Proc. Natl. Acad. Sci. U.S.A.

299

127

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“…Superimposing density maps involves a time-and memoryconsuming multidimensional search (e.g. Bricogne, 1976;Muirhead, Cox, Mazzarella & Perutz, 1967). To sidestep this issue, it is convenient to assume that envelope volumes will be optimally aligned when the protein coordinates from which they are derived are intelligently superimposed.…”

Section: Methodsmentioning

confidence: 99%

A resolution-sensitive procedure for comparing protein surfaces and its application to the comparison of antigen-combining sites

Gerstein¹

1992

Acta Cryst Sect A

109

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HANS GRIMMER 271 and the form of 7r given in Table 3 i.e. only the piezomagnetoelectric effect contributes to PI and P2. Also U2N2P, U2NES, Nb2C0409 and Nb2Mn409 have symmetry 3'm' according to Ole~ et al. (1976).The author is indebted to Professor H. Schmid for his suggestion to investigate the form of the piezomagnetoelectric effect and for stimulating discussions.References AIZU, K. (1970). Phys. Rev. B, 2, 754-772. GRIMMER, H. (1991a). Acta Cryst. A47, 226-232. GRIMMER, H. (1991b). Helv. Phys. Acta, 64, 187-188. KOPSKg, V. (1979 Resolution is a crucial parameter to consider in making surface comparisons. A method is presented here for the rapid, objective and automatic comparison of selected parts of protein surfaces as a function of resolution using differences and correlations of Fourier coefficients. A test-case application of this procedure to the surfaces of five immunoglobulin antigen-combining sites allowed them to be partitioned into two categories.

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“…The mechanism describing the cooperative binding of CO and other ligands to Hb poses a fundamental problem that has not been solved quantitatively (1)(2)(3)(4)(5). To date, the primary methods used to study cooperative effects have been photodissociation and stopped-flow of a steady state of partially or fully ligated Hb.…”

mentioning

confidence: 99%

Picosecond photodissociation and subsequent recombination processes in carbon monoxide hemoglobin.

Noe¹,

Eisert²,

Rentzepis³

1978

Proc. Natl. Acad. Sci. U.S.A.

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ABSTRACrExcitation of HbCO by a single 6-psec 530-nm pulse results in 3hotodissociation with a first-order constant of 0.89 X 1011 sec . The kinetics of photodissociation, monitored by following absorbance changes in the Soret band at 440 nm, are interpreted as corresponding to predissociation followed by a crossing into a dissociative state. Subsequent recombination of CO with the porphyrin system and protein structural transformations were monitored by use of a continuous He-Cd laser beam spatially coincident with the photolysis and Soret interrogation beams at the sample. We find that the latter events take place in three distinct time regions, depending on excitation pulse energy and repetition rate. Excitation of HbCO with a single pulse (0.8-5 mJ) results in a relaxation to the ground state with an associative first-order constant of 5 X 103 sec-1. With a 100-pulse train ("7.5 mj), a new decay grows with a rate constant of 63 sec-1. For a pulse-train energy of 12 mJ or higher, a delay occurs at the onset of the second (slower) recombination.The mechanism describing the cooperative binding of CO and other ligands to Hb poses a fundamental problem that has not been solved quantitatively (1-5). To date, the primary methods used to study cooperative effects have been photodissociation and stopped-flow of a steady state of partially or fully ligated Hb. The subsequent recombination is followed by monitoring optical density changes at suitable wavelengths (6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16). The energetics of ligand-binding in Mb and protoheme have also been investigated by monitoring recombination, after photodissociation, over several orders of magnitude of time (17)(18)(19).The time width of the pulses used for single-pulse excitation cover several ranges: 10-15,sec with flashlamps (9, 10), about 1 usec by flashlamp-pumped dye laser (11)(12)(13)18), and 10 msec with Q-switched solid-state lasers (11,15). Photolysis levels of at least 70% have been reported in most cases.Because the photodissociation of HbCO provides information on the trigger mechanism for the cooperative binding of ligands to Hb, we thought that a more complete wide-range kinetic investigation of the dissociation and recombination of HbCO would be useful. By photodissociation, we do not necessarily imply the removal of CO from the heme pocket. The present work deseribes the photodissociation of HbCO with a single 6-psec 530-nm excitation pulse from a mode-locked Nd+3-glass laser in conjunction with a second analyzing He-Cd laser. The experimental arrangement allows us to monitor, during the course of an experiment, not only the picosecond photodissociation of HbCO at various wavelengths but also the longer process(es) of protein rearrangement and the recombination of CO with Hb. We find that the photodissociation at 40 initiated by the single excitation pulse at 530 nm takes place in 11 psec and follows first-order kinetics. Subsequent events-recombination of CO and protein structural transformationstake place in three distinct time ...

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Structure and function of haemoglobin

Cited by 282 publications

References 14 publications

Glucose-induced conformational change in yeast hexokinase.

Glucose-induced conformational change in yeast hexokinase.

A resolution-sensitive procedure for comparing protein surfaces and its application to the comparison of antigen-combining sites

Picosecond photodissociation and subsequent recombination processes in carbon monoxide hemoglobin.

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