Mice without myoglobin
Article Abstract:
Myoglobin is a haemoprotein which binds molecular oxygen and could help maintain cellular respiration when physiological demands are high. Mice can, however, show normal exercise capacity when they lack myoglobin due to gene knockout technology. These mice are also fertile. They have depigmented soleus and heart muscles but standards muscular performance assays show normal function. Myoglobin does not appear to be necessary during pregnancy and during exercise, and there are unanswered issue raised on metabolic regulation.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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Structure of a ligand-binding intermediate in wild-type carbonnonoxy myoglobin
Article Abstract:
Small molecules including No, O2, CO or H2 are important biological ligands binding to metalloproteins to act in signal transduction, respiration and catalysis. Myoglobin acts as an aid to oxygen diffusion and also binds carbon monoxide. Ligand migration is found to arise via a limited number of pathways involving docking sites. The crystal structure of a ligand-biding intermediate in carbonmonoxy myoglobin is reported.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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Ligand binding and conformational motions in myoglobin
Article Abstract:
X-ray crystallographic investigations of carbon monoxy-myoglobin (MbCO mutant L29W) were undertaken to determine structural changes caused by ligand dissociation. Photodissociated ligands were found to migrate to certain sites in an internal cavity at below 180 K. Photodissociation above 180 K caused ligands to escape from the distal pocket, helped by protein fluctuations.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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