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The role of the distal histidine in myoglobin and haemoglobin

Data up to Jan 2025

Published1988
Citations288
References19

Total Citations Per Year

Abstract

References (19)

Structure and refinement of oxymyoglobin at 1·6 Å resolution

1980 • 641 citations

Structure of human oxyhaemoglobin at 2·1resolution

1983 • 618 citations

Neutron diffraction reveals oxygen–histidine hydrogen bond in oxymyoglobin

1981 • 449 citations

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1987 • 392 citations

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1984 • 374 citations

Synthetic models for the oxygen-binding hemoproteins

1977 • 367 citations

Nature of the Iron–Oxygen Bond in Oxyhæmoglobin

1964 • 360 citations

The molecular basis of blood diseases

1988 • 341 citations

High-level expression of sperm whale myoglobin in Escherichia coli.

1987 • 338 citations

The structure of human carbonmonoxy haemoglobin at 2.7 Å resolution

1980 • 271 citations

Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli.

1985 • 201 citations

Real space refinement of neutron diffraction data from sperm whale carbonmonoxymyoglobin

1981 • 161 citations

Distal residues in the oxygen binding site of haemoglobin studied by protein engineering

1987 • 160 citations

Ligand binding to heme proteins. An evaluation of distal effects.

1983 • 119 citations

[38] Stopped-flow, rapid mixing measurements of ligand binding to hemoglobin and red cells

1981 • 117 citations

The Dissociation of the First Oxygen Molecule from Some Mammalian Oxyhemoglobins

1971 • 106 citations

Properties of the T state of human oxyhemoglobin studies by laser photolysis.

1977 • 104 citations

A Structural Model for the Kinetic Behavior of Hemoglobin

1979 • 97 citations

Rates of isonitrile binding to the isolated alpha and beta subunits of human hemoglobin.

1980 • 39 citations

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The role of the distal histidine in myoglobin and haemoglobin (1988) – Nature | Metascience Observatory Explorer