Examination of intermediates in globular protein unfolding by the tritium labeling method

Volynskaya, A. V.; Kasumov, E. A.; Shishkov, A.V.

doi:10.1134/s107036320711031x

Cited by 2 publications

(3 citation statements)

References 43 publications

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“…According to the data of Kasumov et al ( 1990 ), compression of a protein molecule takes place under low concentration of salts and this effect is associated with the action of anions (Volynskaya et al 2006 , 2007 ). It is known from the work of von Hippel and Schleich ( 1973 ) and Han et al ( 2011 ) that the stabilizing effect of anions is decreased as in the Hofmeister series: citrate > sulfate > phosphate > chloride > nitrate > thiocyanate.…”

Section: Rotation Of the γ-Subunitmentioning

confidence: 99%

A mechano-chemiosmotic model for the coupling of electron and proton transfer to ATP synthesis in energy-transforming membranes: a personal perspective

Kasumov¹,

Kasumov²,

Kasumova³

2014

Photosynth Res

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ATP is synthesized using ATP synthase by utilizing energy either from the oxidation of organic compounds, or from light, via redox reactions (oxidative- or photo phosphorylation), in energy-transforming membranes of mitochondria, chloroplasts, and bacteria. ATP synthase undergoes several changes during its functioning. The generally accepted model for ATP synthesis is the well-known rotatory model (see e.g., Junge et al., Nature 459:364–370, 2009; Junge and Müller, Science 333:704–705, 2011). Here, we present an alternative modified model for the coupling of electron and proton transfer to ATP synthesis, which was initially developed by Albert Lester Lehninger (1917–1986). Details of the molecular mechanism of ATP synthesis are described here that involves cyclic low-amplitude shrinkage and swelling of mitochondria. A comparison of the well-known current model and the mechano-chemiosmotic model is also presented. Based on structural, and other data, we suggest that ATP synthase is a Ca2+/H+–K+ Cl−–pump–pore–enzyme complex, in which γ-subunit rotates 360° in steps of 30°, and 90° due to the binding of phosphate ions to positively charged amino acid residues in the N-terminal γ-subunit, while in the electric field. The coiled coil b2-subunits are suggested to act as ropes that are shortened by binding of phosphate ions to positively charged lysines or arginines; this process is suggested to pull the α3β3-hexamer to the membrane during the energization process. ATP is then synthesized during the reverse rotation of the γ-subunit by destabilizing the phosphated N-terminal γ-subunit and b2-subunits under the influence of Ca2+ ions, which are pumped over from storage—intermembrane space into the matrix, during swelling of intermembrane space. In the process of ATP synthesis, energy is first, predominantly, used in the delivery of phosphate ions and protons to the α3β3-hexamer against the energy barrier with the help of C-terminal alpha-helix of γ-subunit that acts as a lift; then, in the formation of phosphoryl group; and lastly, in the release of ATP molecules from the active center of the enzyme and the loading of ADP. We are aware that our model is not an accepted model for ATP synthesis, but it is presented here for further examination and test.

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Section: Rotation Of the γ-Subunitmentioning

confidence: 99%

A mechano-chemiosmotic model for the coupling of electron and proton transfer to ATP synthesis in energy-transforming membranes: a personal perspective

Kasumov¹,

Kasumov²,

Kasumova³

2014

Photosynth Res

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show abstract

“…For the nonnative conditions the relation between the ASA and the specific radioactivity is given by the expression: s D,i = s N,i + I i /kn i [26]. Here, s N,i and s D,i are the ASA values of the residues under the native and nonnative conditions, respectively; I i is the difference between the corresponding specific radioactivities, and n i is the number of residues of a given type in a globule.…”

Section: Methodsmentioning

confidence: 99%

“…In addition, accessible surface of particular types of amino acid residues may be determined. This allows to reveal the small conformational changes in a protein [25] and to obtain a novel, detailed information on the process of globule unfolding [26].…”

Section: Introductionmentioning

confidence: 99%

An evidence for the equilibrium unfolding intermediates of ribonuclease A by tritium labeling method

Volynskaya

Kasumov

Goldanskii

2006

International Journal of Biological Macromolecules

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Examination of intermediates in globular protein unfolding by the tritium labeling method

Cited by 2 publications

References 43 publications

A mechano-chemiosmotic model for the coupling of electron and proton transfer to ATP synthesis in energy-transforming membranes: a personal perspective

A mechano-chemiosmotic model for the coupling of electron and proton transfer to ATP synthesis in energy-transforming membranes: a personal perspective

An evidence for the equilibrium unfolding intermediates of ribonuclease A by tritium labeling method

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