Characterization of the reaction of methyl acetimidate with sperm whale myoglobin

Biochemistry ◽  
1978 ◽  
Vol 17 (14) ◽  
pp. 2822-2829 ◽  
Author(s):  
Richard D. DiMarchi ◽  
William H. Garner ◽  
Chi-Chin Wang ◽  
George I. H. Hanania ◽  
Frank R. N. Gurd
Keyword(s):  
Sperm Whale ◽  
Sperm Whale Myoglobin

scholarly journals Theoretical Characterization of Carbon Monoxide Vibrational Spectrum in Sperm Whale Myoglobin Distal Pocket

2007 ◽  
Vol 92 (10) ◽  
pp. 3442-3447 ◽  
Author(s):  
Massimiliano Anselmi ◽  
Massimiliano Aschi ◽  
Alfredo Di Nola ◽  
Andrea Amadei
Keyword(s):  
Carbon Monoxide ◽  
Vibrational Spectrum ◽  
Sperm Whale ◽  
Theoretical Characterization ◽  
Sperm Whale Myoglobin

Structural and functional characterization of sperm whale myoglobin mutants: Role of arginine (E10) in ligand stabilization

Biochemistry ◽  
1993 ◽  
Vol 32 (23) ◽  
pp. 6041-6049 ◽  
Author(s):  
Carlo Travaglini Allocatelli ◽  
Francesca Cutruzzola ◽  
Andrea Brancaccio ◽  
Maurizio Brunori ◽  
Jun Qin ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Sperm Whale ◽  
Ligand Stabilization ◽  
Sperm Whale Myoglobin

scholarly journals Functional and structural characterization of the myoglobin from the polychaete Ophelia bicornis

2005 ◽  
Vol 389 (2) ◽  
pp. 497-505 ◽  
Author(s):  
M. Teresa Sanna ◽  
Barbara Manconi ◽  
Massimo Castagnola ◽  
Bruno Giardina ◽  
Daniela Masia ◽  
...  
Keyword(s):  
Oxygen Affinity ◽  
Sperm Whale ◽  
Protein Sequencing ◽  
Oxygen Binding ◽  
Amino Acid Residues ◽  
Experimental Conditions ◽  
The Stability ◽  
Sperm Whale Myoglobin

The myoglobin of the polychaete annelid Ophelia bicornis was isolated, purified to homogeneity and characterized. The primary structure, obtained from cDNA and protein sequencing, consists of 139 amino acid residues. The alignment with other globin sequences showed that O. bicornis myoglobin misses the pre-A helix and the first six residues of the A helix. The presence of a PheB10-GlnE7 haem distal residue pair is in agreement with the measured oxygen affinity (P50=0.85 mmHg; 1 mmHg=0.133 kPa) and the only slightly higher autoxidation rate constant (0.28 h−1) with respect to that of the sperm whale myoglobin mutant E7 His→Gln (0.21 h−1) and to elephant myoglobin (0.1 h−1). Oxygen-binding co-operativity was found to be absent under all the examined experimental conditions. The resistance of O. bicornis myoglobin towards autoxidation seems to confirm the important role of part of the A helix in the stability of the globin. The higher pKa of the acid–alkaline ferric transition of O. bicornis with respect to Asian elephant myoglobin, as well as the higher absorbance ratio of its ferric form to the oxy form measured in the Soret region (γmet/γoxy) with respect to that of the African elephant myoglobin, suggested a stronger interaction between the distal glutamine and the water molecule at the sixth co-ordinate position.

scholarly journals The role of Val68(E11) in ligand binding to sperm whale myoglobin. Site-directed mutagenesis of a synthetic gene.

1990 ◽  
Vol 265 (20) ◽  
pp. 11788-11795
Author(s):  
K D Egeberg ◽  
B A Springer ◽  
S G Sligar ◽  
T E Carver ◽  
R J Rohlfs ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Sperm Whale ◽  
Site Directed Mutagenesis ◽  
Synthetic Gene ◽  
Directed Mutagenesis ◽  
Sperm Whale Myoglobin

The crystal structure of myoglobin. VI. Seal myoglobin

1960 ◽  
Vol 258 (1293) ◽  
pp. 181-201 ◽  
Keyword(s):  
Tertiary Structure ◽  
Heavy Atom ◽  
Three Dimensional ◽  
Sperm Whale ◽  
Fourier Synthesis ◽  
Heavy Atoms ◽  
Isomorphous Replacement ◽  
Unit Cells ◽  
The Common ◽  
Sperm Whale Myoglobin

Myoglobin from the common seal ( Phoca vitulina ) when crystallized from ammonium sulphate forms monoclinic crystals with space group the unit cell, a = 57·9Å, b = 29·6Å, c = 106·4Å, β = 102°15', contains four molecules. The method of isomorphous replacement has been used in an investigation of the centrosymmetric b -axis projection in which it has been possible to determine signs for nearly all the h0l reflexions having spacings greater than 4Å. Three independent heavy-atom derivatives were employed and the signs so determined have been used to compute a map of the electron density projected on the (010) plane. This projection has been interpreted in terms of the molecule of sperm-whale myoglobin, as deduced by Bodo, Dintzis, Kendrew & Wyckoff (1959) from a three-dimensional Fourier synthesis to 6Å resolution. The results of the interpretation show that the two myoglobin molecules are very similar in form (tertiary structure) in spite of the differences in their amino-acid composition. The relative orientation of the two unit cells with respect to the myoglobin molecule is given and a comparison is made of the positions of the heavy atoms in each molecule.

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