ATP synthase: From sequence to ring size to the P/O ratio

Ferguson, Stuart J.

doi:10.1073/pnas.1012260107

Cited by 85 publications

(81 citation statements)

References 14 publications

(11 reference statements)

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“…As shown in Fig. 5C, the c-subunit stoichiometries revealed in unprocessed topographs include c <11 , c 11 , c 12 , c 13 , c 14 , and c >14 . However, the majority of the c-rings consisted of 11, 12, or 13 subunits (52.6%, 33.3%, and 9.6%, respectively) (Fig.…”

Section: Resultsmentioning

confidence: 86%

“…AFM images of c-rings from I. tartaricus, plant chloroplast, and Arthrospira sp. PCC 9438 reveal a unique stoichiometry in each case, namely c 11 , c 14 , and c 15 , respectively. A few c-rings in these images were seen to lack individual c-subunits; however, instead of closing this gap so as to form smaller c-rings, these incomplete oligomers have the same shape and diameter as the complete ones (10,25).…”

Section: Discussionmentioning

confidence: 99%

“…Because the F 1 and F o motors are tightly coupled, the c-ring stoichiometry determines the theoretical ionto-ATP ratio (n/3) of the enzyme, which therefore ranges from 2.7 to 5. This value is also related to the number of ATP molecules synthesized by oxidative phosphorylation for each pair of electrons (the P/O ratio) in respiring mitochondria (14). In sum, the c-ring stoichiometry is an important parameter with direct influence on the cell bioenergetics.…”

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confidence: 99%

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Engineering rotor ring stoichiometries in the ATP synthase

Pogoryelov¹,

Klyszejko

Krasnoselska³

et al. 2012

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

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ATP synthase membrane rotors consist of a ring of c-subunits whose stoichiometry is constant for a given species but variable across different ones. We investigated the importance of c/c-subunit contacts by site-directed mutagenesis of a conserved stretch of glycines (GxGxGxGxG) in a bacterial c 11 ring. Structural and biochemical studies show a direct, specific influence on the c-subunit stoichiometry, revealing c <11 , c 12 , c 13 , c 14 , and c >14 rings. Molecular dynamics simulations rationalize this effect in terms of the energetics and geometry of the c-subunit interfaces. Quantitative data from a spectroscopic interaction study demonstrate that the complex assembly is independent of the c-ring size. Real-time ATP synthesis experiments in proteoliposomes show the mutant enzyme, harboring the larger c 12 instead of c 11 , is functional at lower ion motive force. The high degree of compliance in the architecture of the ATP synthase rotor offers a rationale for the natural diversity of c-ring stoichiometries, which likely reflect adaptations to specific bioenergetic demands. These results provide the basis for bioengineering ATP synthases with customized ion-to-ATP ratios, by sequence modifications.alpha helix packing | F 1 F o ATP synthase | membrane protein | rotary motor stoichiometry | bioenergetics

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Section: Resultsmentioning

confidence: 86%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Engineering rotor ring stoichiometries in the ATP synthase

Pogoryelov¹,

Klyszejko

Krasnoselska³

et al. 2012

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

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“…A TP synthases are conserved, membrane-anchored enzyme complexes that use a rotary-mechanical mechanism to produce ATP, the cell's universal energy currency. The enzymes consist of two major subcomplexes, F 1 (α 3 β 3 γδe) and F o (ab 2 c [8][9][10][11][12][13][14][15] ), which are intimately coupled and driven by the transmembrane electrochemical ion gradient to synthesize three ATP molecules per complete rotation of the rotor, one each in the three (β 3 ) catalytic F 1 sites (1)(2)(3)(4). One part of the enzyme's rotor c n γe, the c-ring (F o rotor ring), is involved in shuttling ions from the outside to the inside of the cell across the membrane by reversible binding and release of ions (H + or Na + ).…”

mentioning

confidence: 99%

“…The number of ions translocated per 360-degree rotation is determined by the c-ring stoichiometry (c n ); thus, the ion-to-ATP ratio, i, of the enzyme is i = c n /β 3 . This bioenergetic cornerstone parameter is known to vary from 2.7 to 5 (11).…”

mentioning

confidence: 99%

The c-ring stoichiometry of ATP synthase is adapted to cell physiological requirements of alkaliphilic Bacillus pseudofirmus OF4

Preiß

Klyszejko

Hicks

et al. 2013

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

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The c-rings of ATP synthases consist of individual c-subunits, all of which harbor a conserved motif of repetitive glycine residues (GxGxGxG) important for tight transmembrane α-helix packing. The cring stoichiometry determines the number of ions transferred during enzyme operation and has a direct impact on the ion-to-ATP ratio, a cornerstone parameter of cell bioenergetics. In the extreme alkaliphile Bacillus pseudofirmus OF4, the glycine motif is replaced by AxAxAxA. We performed a structural study on two mutants with alanine-to-glycine changes using atomic force microscopy and X-ray crystallography, and found that mutants form smaller c 12 rings compared with the WT c 13 . The molar growth yields of B. pseudofirmus OF4 cells on malate further revealed that the c 12 mutants have a considerably reduced capacity to grow on limiting malate at high pH. Our results demonstrate that the mutant ATP synthases with either c 12 or c 13 can support ATP synthesis, and also underscore the critical importance of an alanine motif with c 13 ring stoichiometry for optimal growth at pH >10. The data indicate a direct connection between the precisely adapted ATP synthase c-ring stoichiometry and its ionto-ATP ratio on cell physiology, and also demonstrate the bioenergetic challenges and evolutionary adaptation strategies of extremophiles.

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Reconstruction and analysis of a three‐compartment genome‐scale metabolic model for Pseudomonas fluorescens

Huang

Lin

2020

Biotech and App Biochem

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With the versatile metabolic diversity, Pseudomonas fluorescens is a potential candidate in petroleum aromatic hydrocarbon (PAH) bioremediation. Genome‐scale metabolic model (GSMM) can provide systematic information to guide the development of metabolic engineering strategy to improve microbial activity. In this study, a GSMM for P. fluorescens SBW25 was reconstructed, which is termed as lCW1057. The reconstruction was based on automatic reannotation and manual curation. The periplasmic compartment was constructed to better represent the proton gradient profile. The reconstructed proton transport chain has a P/O (ATP generated per atom oxygen consumed by the respiratory chain) ratio of 11/8. Flux balance analysis (FBA) was performed to explore the whole‐cell metabolic flow. The model suggested that instead of Embden–Meyerhof–Parnas pathway, Entner–Doudoroff pathway was used in glycolytic metabolism of P. fluorescens, indicating that the growth of P. fluorescens is more energy dependent. Furthermore, P. fluorescens can use nitrate as the terminal electron acceptor for the glucose metabolism. The β‐ketoadipate pathway was involved in catechol metabolism. The uptake of oxygen is mandatory for the aromatic ring cleavage. The in silico and in vitro maximum specific growth rate was compared, resulting in 10% difference when catechol was used as the sole carbon source.

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ATP synthase: From sequence to ring size to the P/O ratio

Cited by 85 publications

References 14 publications

Engineering rotor ring stoichiometries in the ATP synthase

Engineering rotor ring stoichiometries in the ATP synthase

The c-ring stoichiometry of ATP synthase is adapted to cell physiological requirements of alkaliphilic Bacillus pseudofirmus OF4

Reconstruction and analysis of a three‐compartment genome‐scale metabolic model for Pseudomonas fluorescens

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