Protons, proteins and ATP

Junge, Wolfgang

doi:10.1007/1-4020-3324-9_53

Cited by 14 publications

(13 citation statements)

References 194 publications

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“…Our work reported here may be regarded as a further development over it, which can now provide a unified framework for understanding the energetics in many biological systems. In addition to explaining the decades-longstanding bioenergetic conundrum in the alkalophilic bacteria, the proton-electrostatics localization hypothesis may also have fundamental implications to better understand the bioenergetics in other biological systems [65][66][67] including (but not limited to) mitochondria [68][69][70][71][72][73] and chloroplasts [74][75][76][77]. It may also help to understand how life began on Earth in relation to the importance of water not only as a solvent and substrate but also as a proton conductor for proton coupling energy transduction.…”

Section: Resultsmentioning

confidence: 99%

Proton-Electrostatic Localization: Explaining the Bioenergetic Conundrum in Alkalophilic Bacteria

Lee¹

2015

Bioenergetics

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Section: Resultsmentioning

confidence: 99%

Proton-Electrostatic Localization: Explaining the Bioenergetic Conundrum in Alkalophilic Bacteria

Lee¹

2015

Bioenergetics

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“…This pathway allows protons in the intermembrane space to access an essential ionized carboxylate of a glutamate residue, midmembrane on the C-terminal α-helix of subunit c. Once protonated, this carboxylate moves to a more hydrophobic environment by Brownian motion generating a rotation of the ring. As succeeding c-subunits become protonated, each neutralized carboxylate reaches an environment in subunit a where it reionises, releasing the proton into the mitochondrial matrix (8). According to current models based on structures, the number of translocated protons for generation of each 360°r otation is the same as the number of c-subunits in the ring, as each c-subunit carries a carboxylate involved in protonation and deprotonation events.…”

mentioning

confidence: 99%

Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria

Watt

Montgomery

Runswick

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

465

417

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The catalytic domain of the F-ATPase in mitochondria protrudes into the matrix of the organelle, and is attached to the membrane domain by central and peripheral stalks. Energy for the synthesis of ATP from ADP and phosphate is provided by the transmembrane proton-motive-force across the inner membrane, generated by respiration. The proton-motive force is coupled mechanically to ATP synthesis by the rotation at about 100 times per second of the central stalk and an attached ring of c-subunits in the membrane domain. Each c-subunit carries a glutamate exposed around the midpoint of the membrane on the external surface of the ring. The rotation is generated by protonation and deprotonation successively of each glutamate. Each 360°rotation produces three ATP molecules, and requires the translocation of one proton per glutamate by each c-subunit in the ring. In fungi, eubacteria, and plant chloroplasts, ring sizes of c 10

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“…(2) The latest descriptions of the structures of components of this mechanism, at atomic resolution, are all consistent with the chemiosmotic theory (for reviews see Refs. 1,[3][4][5]. This theory elevates the status of biological membranes from selective boundaries to active participants in the process of energy conversion.…”

Section: Discussionmentioning

confidence: 98%

Energy transduction anchors genes in organelles

et al. 2005

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The work of mitochondria and chloroplasts is energy transduction in respiration and photosynthesis. The physico-chemical mechanisms of bioenergetics do not directly involve genes and heredity, and furthermore, redox chemistry is intrinsically mutagenic. Thus the small, functional genomes of mitochondria and chloroplasts are an oddity. Although extensively sequenced and catalogued, cytoplasmic genomes are still not explained. Genomic lethargy is not the answer. Some genes linger from the bacterial ancestors of these organelles, true, but most have left, and new ones arrive. There is a mounting case for a massive and indiscriminate intracellular gene transfer between organelles and the cell nucleus, with the frequency of relocation being comparable to that of mutation. Nevertheless, a few organellar proteins, all working at the core of bioenergetics, always seem to keep the genes encoding them close at hand. Stability amid flux suggests the invisible hand of selection. Selection for what? There are clues, and the beginnings of experimental support, for the theory that expression of mitochondrial and chloroplast genes is regulated by the function of their gene products. For safe and efficient energy transduction, genes in organelles are in the right place at the right time.

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Protons, proteins and ATP

Cited by 14 publications

References 194 publications

Proton-Electrostatic Localization: Explaining the Bioenergetic Conundrum in Alkalophilic Bacteria

Proton-Electrostatic Localization: Explaining the Bioenergetic Conundrum in Alkalophilic Bacteria

Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria

Energy transduction anchors genes in organelles

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