Myoglobin is an oxygen-binding haem protein of vertebrate and invertebrate skeletal and cardiac muscle.
Keywords: oxygen-binding haemoprotein; iron protoporphyrin IX
Myoglobin
Koichiro Ishimori, Kyoto University, Kyoto, Japan
Published online: February 2002
DOI: 10.1038/npg.els.0000656
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Figure 1. Globin
fold and haem. A ribbon model of deoxygenated sperm whale myoglobin. The axial
histidine, proximal histidine (His93) and haem are illustrated in the stick
model. A–H, helices.
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Figure 2. Structure
of haem. The numbers represent the positions of the substituents; the
letters A–D show the pyrrole rings. The Greek letters correspond to the meso-positions
of porphyrin.
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Figure 3. Haem
environment of myoglobin. Some amino acid residues located near the haem are
presented. The coordinates are based on deoxygenated sperm whale myoglobin.
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| References | |
| Barrick D (1994) Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93Gly. Biochemistry 33: 6546–6554. | |
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| Inaba K, Ishimori K, Imai K and Morishima I (1998a) Structural and functional effects of pseudo-module substitution in hemoglobin subunits. New structural and functional units in globin structure. Journal of Biological Chemistry 273: 8080–8087. | |
| Inaba K, Ishimori K and Morishima I (1998b) Structural and functional roles of heme binding module in globin proteins: identification of the segment regulating the heme binding structure. Journal of Molecular Biology 283: 311–327. | |
| Kendrew JC, Bodo G, Dintzis HM et al. (1958) A three-dimensional model of the myoglobin molecule obtained by X-ray analysis. Nature 181: 662–666. | |
| La Mar GN, Budd DL and Goff H (1977) Assignment of proximal histidine proton NMR peaks in myoglobin and hemoglobin. Biochemical and Biophysical Research Communications 77: 104–110. | |
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| Further Reading | |
| Barrick D and Baldwin RT (1990) The molten globule intermediate of apomyoglobin and the process of protein folding. Protein Science 2: 869–876. | |
| Springer BA, Sliger SG, Olson JS and Phillips GN Jr (1994) Mechanism of ligand recognition in myoglobin. Chemical Reviews 94: 699–714. | |
| Phillips GN Jr and Pettitt BM (1995) Structure and dynamics of the water around myoglobin. Protein Science 4: 149–158. | |
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Shikama K
(1985)
Nature of the FeO | |
| Wittenberg JB and Wittenberg BA (1990) Mechanisms of cytoplasmic hemoglobin and myoglobin function. Annual Review of Biophysics and Biophysical Chemistry 19: 217–241. | |
