Oligomycin‐sensitive ATPase from beef heart mitochondria: reaction with 2‐mercaptopropionylglycine

Zimmer, G; Mainka, Luise; Ohlenschläger, G

doi:10.1016/0014-5793(78)80942-9

Cited by 17 publications

(5 citation statements)

References 16 publications

(2 reference statements)

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“…It was found that loss of oligomycin-sensitivity was directly correlated with diminution of Band F 0 1 [33]. We have found an analogous increase in oligomycin-sensitivity along with an increase of the 30-31 kDa band induced by MPG [62].…”

Section: Discussionsupporting

confidence: 69%

“…2). Our previous findings [61][62][63][64]20,21,65] using 2-mercapto-propionylglycine (MPG) and the more recent results using alpha lipoic acid [3,11,34,39,47,50,66,68], could, at least in part, become explained by reversible blockade (R-S-MPG; R-S-LA), of reactive sulfhydryl groups at strategic membrane sites including the ATPsynthase with excessive reversible reactivity of the Fo b subunit preserving mobility and structure changes during ATP synthesis.…”

Section: Discussionmentioning

confidence: 83%

“…As is becoming evident from the foregoing discussion, in mitochondria, oligomycin -sensitive thiol reactivity occurs to a remarkable extent [1,4,7,8,[18][19][20]33,43,57,58,61,62,64,66]. Such mitochondrial -SH reactivity can be also deduced to working rat hearts in experimentation with MPG [65] and alpha lipoic acid [67].…”

Section: Discussionmentioning

confidence: 99%

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ADP‐ and oligomycin‐sensitive redox behavior of F₀ b thiol in ATPsynthase depends on neighbored primary structure: Investigations using 14‐C‐labeled alpha lipoic acid

Dünschede¹,

Zwicker

Ackermann

et al. 2003

BioFactors

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Purified ATPsynthase of bovine heart mitochondria has been analyzed for its mobility and reactivity of oligomycin-sensitive sulfhydryl regions in presence of the substrate ADP and oligomycin. Labeling of thiol groups at the hydrophobic F_0 region of the ATPsynthase was increased in the enzyme initially treated with SDS, N-ethylmaleimide and dithiothreitol (modified enzyme). After dialysis or gel permeation the ATPsynthase was treated with [14C] alpha lipoic acid at a molar ratio of 35-85/1 (lipoic acid/ATPsynthase) corresponding to 4-8.6 nmol/mg protein. Under these conditions, ATPase activity of the native enzyme was significantly decreased. After preincubation with ADP, PAGE of the native, [14C] labeled enzyme revealed an increase of radioactivity at a region of 25 kDa deduced to Cys 197 of subunit b. In the modified enzyme the increase in radioactivity was found at 10 kDa. In this context, the sequence Lys-Cys-Ile around Cys 197 of subunit b suggests excessive reactivity of this thiol, as well as ready reversibility by -SH-S-S- interchange. Therefore, previously observed reaction by thiol reagents and antioxidants from outside the mitochondrion can be interpreted with Cys 197 of F0 b. It accounts for sulfhydryl unmasked by binding of ADP at F1.

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Section: Discussionsupporting

confidence: 69%

Section: Discussionmentioning

confidence: 83%

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ADP‐ and oligomycin‐sensitive redox behavior of F₀ b thiol in ATPsynthase depends on neighbored primary structure: Investigations using 14‐C‐labeled alpha lipoic acid

Dünschede¹,

Zwicker

Ackermann

et al. 2003

BioFactors

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“…In the Iowermolecular-mass region several bands are visible that could be attributed to the F, part of the ATPase complex [25], although a recent report suggests that only one of these bands is an [28]. The clear bands at 28 k D a and 30 k D a are not identified, but are also obvious companions in other ATPase complex preparations [17,27, and are interpreted as integral parts of the FIFO ATPase [16,17,27,29,30,321, as impurities [16,321 or as polymers of low-molecularmass components of the complex [31].…”

Section: Discussionmentioning

confidence: 87%

Isolation, purification and characterization of the ATPase complex from the thermophilic cyanobacterium Synechococcus 6716

Lubberding

Zimmer

Walraven

et al. 1983

European Journal of Biochemistry

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The ATPase complex is isolated and purified from membrane vesicles of the thermophilic cyanobacterium Synechococcus 6716 by octyl glucoside and cholic acid by a modification of the procedure for its extraction from spinach chloroplasts. The complex is purified by differential centrifugation and ammonium sulfate precipitation and by gel filtration on Sepharose 6B. The purified fraction, without any phycocyanin contamination, shows ATP hydrolysis activity and Pi/ATP exchange activity of 1564 and 350 nmol · min−1· mg protein−1, respectively. N, N′‐Dicyclohexylcarbodiimide inhibits the ATP hydrolysis activity of this purified fraction. On polyacrylamide gels most typical F1 ATPase polypeptides are identified, but the low‐molecular weight polypeptides visible cannot be ascribed to the Fo part of the complex with certainty; non‐identified bands around 30kDa are also present.

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“…Electron-microscopically, the appearance of mitochondria in the presence of MPG resembled that found in the presence of ADP (27,34), i.e., condensed forms become visible. In OS-ATPase from beef heart mitochondria, the 28-31 ka protein rose in staining intensity along with low molecular weight (8-15 kd) proteins (36). Further discussion on interrelations of these proteins has been carried out by Terada (30) and others (1,4,26,38).…”

Section: Structural Findings With Mpgmentioning

confidence: 95%

Uncoupler- and hypoxia-induced damage in the working rat heart and its treatment

1985

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In the working rat heart we investigated heart function (aortic and coronary flow) during a normoxic, a hypoxic, and a reoxygenation phase after hypoxia. A depressed heart function was obtained by limiting oxygen supply and reducing left ventricular filling pressure (preload). After hypoxic perfusion for about 90 min, reoxygenation resulted in a 50% decrease of aortic flow. Lactate production and release increased immediately after oxygen deprivation and reached a maximum after about 35 min of hypoxia. Following reoxygenation, lactate release decreased. Lactate dehydrogenase became significant after reoxygenation. After stabilization of aortic flow at 50% in the reoxygenation phase different reagents were examined for their influence on heart performance. 1.5 mM of 2-Mercaptopropionylglycine (MPG) significantly increased aortic flow by 40%. The oxidized form of MPG (ox-MPG) at a concentration of 0.6 mM increased aortic flow by 125%. A molecular mechanism is proposed involving reorientation of the ATPase molecules at their membrane sites.

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Oligomycin‐sensitive ATPase from beef heart mitochondria: reaction with 2‐mercaptopropionylglycine

Cited by 17 publications

References 16 publications

ADP‐ and oligomycin‐sensitive redox behavior of F₀ b thiol in ATPsynthase depends on neighbored primary structure: Investigations using 14‐C‐labeled alpha lipoic acid

ADP‐ and oligomycin‐sensitive redox behavior of F₀ b thiol in ATPsynthase depends on neighbored primary structure: Investigations using 14‐C‐labeled alpha lipoic acid

Isolation, purification and characterization of the ATPase complex from the thermophilic cyanobacterium Synechococcus 6716

Uncoupler- and hypoxia-induced damage in the working rat heart and its treatment

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Oligomycin‐sensitive ATPase from beef heart mitochondria: reaction with 2‐mercaptopropionylglycine

Cited by 17 publications

References 16 publications

ADP‐ and oligomycin‐sensitive redox behavior of F0 b thiol in ATPsynthase depends on neighbored primary structure: Investigations using 14‐C‐labeled alpha lipoic acid

ADP‐ and oligomycin‐sensitive redox behavior of F0 b thiol in ATPsynthase depends on neighbored primary structure: Investigations using 14‐C‐labeled alpha lipoic acid

Isolation, purification and characterization of the ATPase complex from the thermophilic cyanobacterium Synechococcus 6716

Uncoupler- and hypoxia-induced damage in the working rat heart and its treatment

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Product

Resources

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ADP‐ and oligomycin‐sensitive redox behavior of F₀ b thiol in ATPsynthase depends on neighbored primary structure: Investigations using 14‐C‐labeled alpha lipoic acid

ADP‐ and oligomycin‐sensitive redox behavior of F₀ b thiol in ATPsynthase depends on neighbored primary structure: Investigations using 14‐C‐labeled alpha lipoic acid