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Effect of artificial and natural phospholipid membranes on rate of sperm whale oxymyoglobin autooxidation

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Abstract

We were the first to show that MbO2 deoxygenation in the cell occurs only upon interaction of myoglobin with mitochondrial membrane, which must be accompanied by changes in the heme cavity conformation of the protein and its affinity for the ligand. Under aerobic conditions, some changes in the equilibrium O2 dissociation constant (K dis) can be detected by changes of the rate of MbO2 autooxidation, i.e. spontaneous turning it into metMb (k ox), as far as a direct correlation between K dis and k ox is experimentally shown. In this work, we studied the effect on MbO2 autooxidation rate of phospholipid liposomes from neutral soybean phosphatidylcholine (lecithin) and from negatively charged 1-palmitoyl-2-oleylphosphatidylglycerol (POPG) at various phospholipid/MbO2 ratios from 25 : 1 to 100 : 1, and also the effect of rat liver mitochondria at concentration of 1 and 2 mg/ml mitochondrial protein (at 22 and 37°C). In all cases, k ox was found to increase due to interaction of the protein with phospholipid membranes. The effect of negatively charged liposomes from POPG on kox is significantly greater than that of neutral lecithin liposomes. At the POPG/MbO2 molar ratio of 25 : 1, MbO2 autooxidation rate is almost 25-fold increased compared to the control, whereas in the presence of 50-fold molar excess of lecithin, k ox is only ∼10 times higher (10 mM buffer, pH 7.2, 22°C). With the same phospholipid/MbO2 ratio of 100: 1, k ox is 7 times higher for the POPG than for lecithin liposomes. In the presence of mitochondria inhibited by antimycin A, k ox grows proportionally to their concentration (about 10-fold per 1 mg/ml of mitochondrial protein), and practically does not change after adding superoxide dismutase in the reaction mixture. The k ox value decreases markedly at high ionic strength, thus suggesting an important role of coulombic electrostatics in the myoglobin-mitochondrial interaction. The increase in the autooxidation rate of MbO2 (and hence its K dis) due to the interaction with phospholipid membranes points to decreasing affinity of myoglobin for oxygen, which facilitates O2 detachment from MbO2 at physiological p 02 values.

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Abbreviations

te]HbO2 :

oxyhemoglobin

K dis :

equilibrium O2 dissociation constant

K m :

constant of myoglobin binding with phospholipid membranes

k ox :

constant of MbO2 autooxidation rate

M 540:

merocyanine 540

MbO2 :

oxymyoglobin

metMb:

metmyoglobin

p 02 :

partial oxygen pressure

POPG:

1-palmitoyl-2-oleylphosphatidylglycerol

SOD:

superoxide dismutase

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Authors and Affiliations

  1. Institute of Cell Biophysics, Russian Academy of Sciences, ul. Institutskaya 3, 142290, Pushchino, Moscow Region, Russia

    G. B. Postnikova & E. A. Shekhovtsova

Authors
  1. G. B. Postnikova
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  2. E. A. Shekhovtsova
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Correspondence to G. B. Postnikova.

Additional information

Published in Russian in Biokhimiya, 2013, Vol. 78, No. 3, pp. 357–363.

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Postnikova, G.B., Shekhovtsova, E.A. Effect of artificial and natural phospholipid membranes on rate of sperm whale oxymyoglobin autooxidation. Biochemistry Moscow 78, 267–272 (2013). https://doi.org/10.1134/S0006297913030085

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  • DOI: https://doi.org/10.1134/S0006297913030085

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