Kinetics of conformation change of sperm-whale myoglobin. II. Characterization of the rapidly and slowly formed denatured species (D and D*)

Biochemistry ◽  
1972 ◽  
Vol 11 (10) ◽  
pp. 1842-1844 ◽  
Author(s):  
Linus L. Shen ◽  
Jan Hermans
Keyword(s):  
Sperm Whale ◽  
Conformation Change ◽  
Kinetics Of ◽  
Sperm Whale Myoglobin

scholarly journals Functional consequences of haem orientational disorder in sperm-whale and yellow-fin-tuna myoglobins

1987 ◽  
Vol 243 (1) ◽  
pp. 205-210 ◽  
Author(s):  
H S Aojula ◽  
M T Wilson ◽  
I E G Morrison
Keyword(s):  
Ligand Binding ◽  
Kinetic Parameters ◽  
Sperm Whale ◽  
Binding Kinetics ◽  
Orientational Disorder ◽  
Binding Properties ◽  
Functional Consequences ◽  
Kinetics Of ◽  
Sperm Whale Myoglobin ◽  
O2 Dissociation

Ligand-binding kinetics of native and reconstituted sperm-whale myoglobin were studied in relation to haem orientational disorder by rapid kinetic methods. In addition, native yellow-fin-tuna myoglobin with significant amount of haem disorder was also used. The O2 dissociation and association rates were found for the proteins with different degrees of haem disorder, and these results suggest that the isomers are characterized by almost identical kinetic parameters. Rates of CO recombination after photolysis were also identical for the two orientational isomers. The results clearly indicate that the rotation of the haem about the alpha-gamma meso axis has little or no effect on the ligand-binding properties of these myoglobins.

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.

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
Sign in / Sign up

Export Citation Format

Share Document