منابع مشابه
The leghemoglobin proximal heme pocket directs oxygen dissociation and stabilizes bound heme.
Sperm whale myoglobin (Mb) and soybean leghemoglobin (Lba) are two small, monomeric hemoglobins that share a common globin fold but differ widely in many other aspects. Lba has a much higher affinity for most ligands, and the two proteins use different distal and proximal heme pocket regulatory mechanisms to control ligand binding. Removal of the constraint provided by covalent attachment of th...
متن کاملEPR characterization of the stereochemistry of the distal heme pocket of the engineered human myoglobin mutants.
Recombinant human myoglobin mutants with the distal histidine residue replaced by Leu, Val, or Gln residues have been prepared by site-directed mutagenesis and expression in Escherichia coli. The recombinant apomyoglobin proteins have been successfully reconstituted with cobaltous protoporphyrin IX to obtain cobalt myoglobin mutant proteins, and the role of the distal histidine residue on the i...
متن کاملFunctional analysis of the iron(II) etiocorrphycene incorporated in the myoglobin heme pocket.
The iron(III) complex of 2,7,12,17-tetraethyl-3,6,11,18-tetra-methylcorrphycene, an isomeric heme, was complexed with apomyoglobin to examine the ligand binding ability of the novel macrocycle under physiological conditions. The reconstituted holoprotein was found to be functionally active at pH 7.4 and 20 degrees C and to bind oxygen and carbon monoxide reversibly with a half-saturation pressu...
متن کاملFilling Up the Heme Pocket Stabilizes Apomyoglobin and Speeds Up Its Folding
Wild type apomyoglobin folds in at least two steps: the ABGH core rapidly, followed much later by the heme-binding CDEF core. We hypothesize that the evolved heme-binding function of the CDEF core frustrates its folding: it has a smaller contact order and is no more complex topologically than ABGH, and thus, it should be able to fold faster. Therefore, filling up the empty heme cavity of apomyo...
متن کاملAccessibility of oxygen with respect to the heme pocket in horseradish peroxidase.
Oxygen and other molecules of similar size take part in a variety of protein reactions. Therefore, it is critical to understand how these small molecules penetrate the protein matrix. The protein system studied in this case is horseradish peroxidase (HRP). We have converted the native HRP into a phosphorescent analog by replacing the heme prosthetic group by Pd-mesoporphyrin. Oxygen readily que...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2001
ISSN: 0021-9258
DOI: 10.1074/jbc.m008593200