Membrane-binding and lipid vesicle cross-linking kinetics of the mitochondrial creatine kinase octamer

Biochemistry
O StachowiakT Wallimann

Abstract

Mitochondrial creatine kinase (Mi-CK; EC 2.7.3.2) is a positively charged enzyme located between the mitochondrial inner and outer membrane as well as along the cristae membranes. The octameric form of Mi-CK is able to cross-link membranes to form contact sites. The process of Mi-CK membrane binding and Mi-CK-induced cross-linking of model membrane vesicles containing different amounts of cardiolipin (CL) was investigated in vitro. First, the direct binding of octameric Mi-CK to immobilized lipid vesicles containing cardiolipin was monitored by plasmon resonance (BiaCore). The analysis of the pseudo-first-order on- and off-rate constants indicates that there are two binding sites with different affinity for Mi-CK on the membrane. The association equilibrium constants obtained at 25 degrees C were 813.7 (for 100% CL) and 343.6 (for 16% CL), respectively, for the high-affinity binding mode. Second, the Mi-CK-induced vesicle cross-linking kinetics were analyzed by fixed-angle light scattering. Only octameric Mi-CK induced bridged vesicle/protein complexes, whereas dimeric Mi-CK failed to induce vesicle cross-linking. For vesicles containing 100% cardiolipin, the pseudo-first-order association rate constant was 2.55 x 10(-3) s-1, w...Continue Reading

References

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Citations

Mar 31, 2011·Amino Acids·Theo WallimannUwe Schlattner
Oct 29, 1998·Journal of Chromatography. B, Biomedical Sciences and Applications·D R Hall, D J Winzor
Jan 22, 1998·Current Opinion in Structural Biology·W Kabsch, K Fritz-Wolf
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May 5, 2009·Biochimica Et Biophysica Acta·Uwe SchlattnerRichard M Epand
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Mar 27, 2004·The Journal of Biological Chemistry·Uwe SchlattnerTheo Wallimann
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Jun 27, 1998·The Journal of Biological Chemistry·O StachowiakC Richter
Jul 19, 2001·Physiological Genomics·F KernecA P Koretsky

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