Functional properties of native and reconstituted hemoglobins from Chironomus thummi thummi.

A procedure for preparation of native globin from Chironomus hemoglobin has been developed and functional properties of native and reconstituted (proto-, meso- and deutero-) hemoglobins have been studied. Globin differs from the corresponding hemoglobin in a number of properties, but the differences are reversible and vanish on addition of protoheme. The oxygen affinity of protohemoglobin (p1/2 = 0.7 mm Hg at 20°C) is lower than that of meso- and deutero-hemoglobins, respectively, the shape of oxygenation curve of all three hemoproteins being consistent with a simple mass-law formulation. While protohemoglobin shows a small but definite Bohr effect, the oxygen affinity of the deuteroderivative is pH independent. Kinetic results show that binding of oxygen, carbon monoxide and ethylisocyanide to native and reconstituted Chironomus hemoglobins is a simple process, since the association process follows bimolecular behaviour and the dissociation reaction conforms to first-order kinetics.

[1]  M H SMITH,et al.  Kinetics and equilibria in systems containing haem, carbon monoxide and pyridine. , 1959, The Biochemical journal.

[2]  F. Jung,et al.  Kinetik der Dissoziation von Alkylisocyanidkomplexen monomerer und oligomerer Hämoglobine , 1972 .

[3]  H. Sick,et al.  Die O2‐Bindungseigenschaften einiger Larvalhamoglobine von Chironomus th. thummi , 1969 .

[4]  R. Crichton,et al.  [Hemoglobins. XV. On monomeric and dimeric insect hemoglobins (Chironomus thummi)]. , 1968, Hoppe-Seyler's Zeitschrift fur physiologische Chemie.

[5]  Erdman Jg,et al.  The nature of the non-porphyrin bonding in derivatives of ferriheme. , 1947 .

[6]  R. Huber,et al.  Structures of deoxy- and carbonmonoxy-erythrocruorin. , 1970, Journal of molecular biology.

[7]  J. Engel,et al.  Optical rotatory dispersion of a respiratory hemeprotein of Chrinomus thummi , 1968 .

[8]  M. Brunori,et al.  Kinetic studies of ligand binding to hemoglobin and its isolated subunits by the temperature jump relaxation method. , 1969, The Journal of biological chemistry.

[9]  W. Hoppe,et al.  Chemische und röntgenographische Untersuchungen am Erythrocruorin , 1964 .

[10]  E. Antonini,et al.  Studies on the oxygen and carbon monoxide equilibria of human myoglobin. , 1958, Archives of biochemistry and biophysics.

[11]  J. Wittenberg,et al.  Myoglobin-facilitated oxygen diffusion: role of myoglobin in oxygen entry into muscle. , 1970, Physiological reviews.

[12]  E. Antonini.  The Reactions of the Isolated a and p Chains of Human Hemoglobin with Oxygen and Carbon Monoxide * , 2003 .

[13]  K. D. Hardman,et al.  RELATIVE CONFORMATIONS OF SPERM WHALE METMYOGLOBIN AND APOMYOGLOBIN IN SOLUTION. , 1965, The Journal of biological chemistry.

[14]  H Formanek,et al.  The atomic structure of erythrocruorin in the light of the chemical sequence and its comparison with myoglobin. , 1971, European journal of biochemistry.

[15]  E. Antonini,et al.  Studies on the structure of hemoglobin. I. Physicochemical properties of human globin. , 1958, Biochimica et biophysica acta.

[16]  E. Blout,et al.  REVERSIBLE CONFORMATIONAL CHANGES OF MYOGLOBIN AND APOMYOGLOBIN. , 1965, The Journal of biological chemistry.

[17]  K. Gersonde,et al.  Heterotropic allosterism of monomeric haemoglobins of Chironomus thummi thummi. , 1972, European journal of biochemistry.

[18]  Q H Gibson,et al.  Apparatus for rapid and sensitive spectrophotometry. , 1964, The Biochemical journal.

[19]  M. Brunori,et al.  Primary structure of aplysia myoglobin: Sequence of a 63‐residue fragment , 1971, FEBS letters.

[20]  F. Roughton,et al.  The kinetics of dissociation of the first oxygen molecule from fully saturated oxyhaemoglobin in sheep blood solutions , 1955, Proceedings of the Royal Society of London. Series B - Biological Sciences.

[21]  M. Brunori,et al.  Studies on the reaction of isocyanides with haemproteins. II. Binding to normal and modified human haemoglobins. , 1972, Journal of molecular biology.

[22]  B. Wittenberg,et al.  The kinetics of the reactions of leghemoglobin with oxygen and carbon monoxide. , 1972, The Journal of biological chemistry.

[23]  M. Brunori,et al.  Studies on the relations between molecular and functional properties of hemoglobin. VI. Observations on the kinetics of hemoglobin reactions in concentrated salt solutions. , 1967, The Journal of biological chemistry.