A naturally occurring mutation in ATP synthase subunit c is associated with increased damage following hypoxia/reoxygenation in STEMI patients

In eukaryotic and prokaryotic cells, F-ATP synthases provide energy through the synthesis of ATP. The chloroplast F-ATP synthase (CF1FO-ATP synthase) of plants is integrated into the thylakoid membrane via its FO-domain subunits a, b, b’ and c. Subunit c with a stoichiometry of 14 and subunit a form the gate for H+-pumping, enabling the coupling of electrochemical energy with ATP synthesis in the F1 sector. Here we report the crystallization and structure determination of the c14-ring of subunit c of the CF1FO-ATP synthase from spinach chloroplasts. The crystals belonged to space group C2, with unit-cell parameters a=144.420, b=99.295, c=123.51 Å, and β=104.34° and diffracted to 4.5 Å resolution. Each c-ring contains 14 monomers in the asymmetric unit. The length of the c-ring is 60.32 Å, with an outer ring diameter 52.30 Å and an inner ring width of 40 Å.

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Biological-to-electronic interface with pores of ATP synthase subunit C in silicon nitride barrier

Medical & Biological Engineering & Computing ◽

10.1007/bf02344699 ◽

2000 ◽

Vol 38 (1) ◽

pp. 113-119 ◽

Cited By ~ 10

Author(s):

J. E. M. McGeoch ◽

M. W. McGeoch ◽

D. J. D. Carter ◽

R. F. Shuman ◽

G. Guidotti

Keyword(s):

Silicon Nitride ◽

Atp Synthase ◽

Subunit C ◽

Electronic Interface

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Influence of subunit-specific antibodies on the activity of the F0 complex of the ATP synthase of Escherichia coli. II. Effects of subunit c-specific polyclonal antibodies.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)49849-9 ◽

1992 ◽

Vol 267 (17) ◽

pp. 12370-12374

Author(s):

G Deckers-Hebestreit ◽

K Altendorf

Keyword(s):

Escherichia Coli ◽

Atp Synthase ◽

Polyclonal Antibodies ◽

Subunit C ◽

Specific Antibodies

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LONG-TERM FIBROBUST CULTURES FROM NEURONAL CEROID LIPOFUSCINOSIS AND MUCOPOLYSACCHARIDOSIS CASES DO NOT SHOW INCREASED EXPRESSION OF SUBUNIT C OF MITOCHONDFUAL ATP SYNTHASE

Journal of Neuropathology & Experimental Neurology ◽

10.1097/00005072-199305000-00085 ◽

1993 ◽

Vol 52 (3) ◽

pp. 281

Author(s):

E. Kida ◽

K. E. Wisniewski

Keyword(s):

Atp Synthase ◽

Neuronal Ceroid Lipofuscinosis ◽

Subunit C ◽

Ceroid Lipofuscinosis

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Topographic variabilities of immunoreactivity to subunit c of mitochondrial ATP synthase and lectin binding in late infantile neuronal ceroid-lipofuscinosis

American Journal of Medical Genetics ◽

10.1002/ajmg.1320570215 ◽

1995 ◽

Vol 57 (2) ◽

pp. 182-186 ◽

Cited By ~ 13

Author(s):

Elzbieta Kida ◽

Krystyna E. Wisniewski ◽

Fred Connell

Keyword(s):

Atp Synthase ◽

Neuronal Ceroid Lipofuscinosis ◽

Lectin Binding ◽

Subunit C ◽

Infantile Neuronal Ceroid Lipofuscinosis ◽

Ceroid Lipofuscinosis ◽

Mitochondrial Atp Synthase

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Reversible Thiol Oxidation Inhibits the Mitochondrial ATP Synthase in Xenopus laevis Oocytes

Antioxidants ◽

10.3390/antiox9030215 ◽

2020 ◽

Vol 9 (3) ◽

pp. 215 ◽

Cited By ~ 3

Author(s):

James Cobley ◽

Anna Noble ◽

Rachel Bessell ◽

Matthew Guille ◽

Holger Husi

Keyword(s):

Xenopus Laevis ◽

Atp Synthase ◽

Xenopus Laevis Oocytes ◽

Proton Pumps ◽

Thiol Oxidation ◽

Protein Thiol ◽

Complex Iv ◽

Subunit C ◽

Catalyst Free ◽

Mitochondrial Atp Synthase

Oocytes are postulated to repress the proton pumps (e.g., complex IV) and ATP synthase to safeguard mitochondrial DNA homoplasmy by curtailing superoxide production. Whether the ATP synthase is inhibited is, however, unknown. Here we show that: oligomycin sensitive ATP synthase activity is significantly greater (~170 vs. 20 nmol/min−1/mg−1) in testes compared to oocytes in Xenopus laevis (X. laevis). Since ATP synthase activity is redox regulated, we explored a regulatory role for reversible thiol oxidation. If a protein thiol inhibits the ATP synthase, then constituent subunits must be reversibly oxidised. Catalyst-free trans-cyclooctene 6-methyltetrazine (TCO-Tz) immunocapture coupled to redox affinity blotting reveals several subunits in F1 (e.g., ATP-α-F1) and Fo (e.g., subunit c) are reversibly oxidised. Catalyst-free TCO-Tz Click PEGylation reveals significant (~60%) reversible ATP-α-F1 oxidation at two evolutionary conserved cysteine residues (C244 and C294) in oocytes. TCO-Tz Click PEGylation reveals ~20% of the total thiols in the ATP synthase are substantially oxidised. Chemically reversing thiol oxidation significantly increased oligomycin sensitive ATP synthase activity from ~12 to 100 nmol/min−1/mg−1 in oocytes. We conclude that reversible thiol oxidation inhibits the mitochondrial ATP synthase in X. laevis oocytes.

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