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  • 1
    Electronic Resource
    Electronic Resource
    Hexokinase receptor complex in hepatoma mitochondria: evidence from N,N'-dicyclohexlycarbodiimide-labeling studies for the involvement of the pore-forming protein VDAC (1986)
    s.l. : American Chemical Society
    Biochemistry 25 (1986), S. 1015-1021 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00353a010
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  • 2
    Electronic Resource
    Electronic Resource
    STRUCTURE AND MODE OF ACTION OF A VOLTAGE DEPENDENT ANION-SELECTIVE CHANNEL (VDAC) LOCATED IN THE OUTER MITOCHONDRIAL MEMBRANE DEPENDENT ANION-SELECTIVE CHANNEL (VDAC) (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 341 (1980), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1980.tb47198.x
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  • 3
    Electronic Resource
    Electronic Resource
    Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained from paramecium mitochondria (1976)
    Springer
    The journal of membrane biology 30 (1976), S. 99-120 
    Details
    ISSN: 1432-1424
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary We have incorporated into planar lipid bilayer membranes a voltage-dependent, anion-selective channel (VDAC) obtained fromParamecium aurelia. VDAC-containing membranes have the following properties: (1) The steady-state conductance of a many-channel membrane is maximal when the transmembrane potential is zero and decreases as a steep function of both positive and negative voltage. (2) The fraction of time that an individual channel stays open is strongly voltage dependent in a manner that parallels the voltage dependence of a many-channel membrane. (3) The conductance of the open channel is about 500 pmho in 0.1 to 1.0m salt solutions and is ohmic. (4) The channel is about 7 times more permeable to Cl− than to K+ and is impermeable to Ca++. The procedure for obtaining VDAC and the properties of the channel are highly reproducible. VDAC activity was found, upon fractionation of the paramecium membranes, to come from the mitochondria. We note that the published data on mitochondrial Cl− permeability suggest that there may indeed be a voltage-dependent Cl− permeability in mitochondria. The method of incorporating VDAC into planar lipid bilayers may be generally useful for reconstituting biological transport systems in these membranes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01869662
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  • 4
    Electronic Resource
    Electronic Resource
    Purification of VDAC (Voltage-dependent anion-selective channel) from rat liver mitochondria (1983)
    Springer
    The journal of membrane biology 74 (1983), S. 115-121 
    Details
    ISSN: 1432-1424
    Keywords: channel ; voltage-dependence outer membrane ; mitochondrion ; VDAC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The outer membrane of rat liver mitochondria contains a channel-forming protein known as VDAC (voltage-dependent anion-selective channel). This protein has been functionally purified by a combination of ion exchange chromatography, gel filtration and affinity chromatography on a Concanavalin A-containing column. An estimated 300-fold purification was achieved over the specific activity in mitochondrial membranes. When the purified protein is run on an SDS polyacrylamide gel, essentially only one band is present at a position consistent with a molecular weight of 32,000. The resulting protein is functional and behaves normally based on channel size, selectivity and voltage dependence.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01870500
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  • 5
    Electronic Resource
    Electronic Resource
    Evidence for titratable gating charges controlling the voltage dependence of the outer mitochondrial membrane channel, VDAC (1985)
    Springer
    The journal of membrane biology 86 (1985), S. 51-59 
    Details
    ISSN: 1432-1424
    Keywords: membrane protein ; pore ; protein modification ; gating mechanism ; planar bilayer membrane ; protein titration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A voltage-dependent anion-selective channel, VDAC, is found in outer mitochondrial membranes. VDAC's conductance is known to decrease as the transmembrane voltage is increased in either the positive or negative direction. Charged groups on the channel may be responsible for this voltage dependence by allowing the channel to respond to an applied electric field. If so, then neutralization of these charges would eliminate the voltage dependence. Channels in planar lipid bilayers which behaved normally at pH 6 lost much of their voltage dependence at high pH. Raising the pH reduced the steepness of the voltage dependence and raised the voltage needed to close half the channels. In contrast, the energy difference between the open and closed state in the absence of a field was changed very little by the elevated pH. The groups being titrated had an apparent pK of 10.6. From the pK and chemical modification, lysine epsilon amino groups are the most likely candidates responsible for VDAC's ability to respond to an applied electric field.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01871610
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  • 6
    Electronic Resource
    Electronic Resource
    Voltage dependence and ion selectivity of the mitochondrial channel, VDAC, are modified by succinic anhydride (1985)
    Springer
    The journal of membrane biology 83 (1985), S. 81-86 
    Details
    ISSN: 1432-1424
    Keywords: voltage-gating ; outer membrane ; membrane ; ion transport ; protein modification ; planar bilayer membrane
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The mitochondrial protein VDAC forms voltage-dependent anion-selective channels in planar phospholipid membranes. When succinic anhydride was added to these membranes, it virtually eliminated VDAC's voltage-dependence and changed its selectivity from anion to cation. These results were obtained without large changes in open-channel conductance or in energy difference between the open and closed states in the absence of a field. Since succinic anhydride converts amino groups into carboxyl groups, we propose that amino groups are responsible for VDAC's voltage-dependence and anion selectivity. Perhaps the same charges are responsible for both functions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01868740
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  • 7
    Electronic Resource
    Electronic Resource
    The mitochondrial voltage-dependent channel, VDAC, is modified asymmetrically by succinic anhydride (1985)
    Springer
    The journal of membrane biology 83 (1985), S. 87-94 
    Details
    ISSN: 1432-1424
    Keywords: voltage-gating ; protein modification ; mechanism ; planar lipid membrane ; outer membrane ; ion transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary In the accompanying paper, succinic anhydride was shown to react with the outer mitochondrial membrane channel-forming protein, VDAC, resulting in the loss of its voltage dependence. In this paper, the anhydride was added to VDAC held in a particular conformational state by means of an applied electric field. VDAC was inserted into the membranes from thecis side and the anhydride was added either to thecis ortrans side. Channels modified in the open state behaved similarly whether anhydride was added to thecis ortrans side. Modifications of VDAC in either of the two closed states did not. Modifications resulting in the loss of voltage-dependence occurred primarily when anhydride was added to the negative side of the membrane irrespective of which closed state the VDAC was in indicating that the accessibility of the gating charges alternated between thecis andtrans sides as the channel's conformation was changed from one closed state to the other. Despite the pronounced asymmetry, in general the resulting channels behaved in the same way in response to either positive or negative fields. A model consistent with the results is presented which proposes that the same gating charges are responsible for channel closure at both positive and negative fields.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01868741
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  • 8
    Electronic Resource
    Electronic Resource
    Voltage gating in the mitochondrial channel, VDAC (1989)
    Springer
    The journal of membrane biology 111 (1989), S. 103-111 
    Details
    ISSN: 1432-1424
    Keywords: channel ; VDAC ; voltage gating ; mitochondria ; outer membrane ; protein structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01871775
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  • 9
    Electronic Resource
    Electronic Resource
    Channel formation in phospholipid bilayer membranes by the toxin ofHeminthosporium maydis, race T (1985)
    Springer
    The journal of membrane biology 87 (1985), S. 151-157 
    Details
    ISSN: 1432-1424
    Keywords: host-specific pathotoxin ; ionophore ; cations ; permeability ; corn
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Southern Corn Leaf Blight is caused by a toxin produced by a virulent form ofHelminthosporium maydis (Race T). The toxin has been shown to uncouple oxidative phosphorylation and dissipate Ca2+ gradients in mitochondria isolated from susceptible, but not resistant, corn. The possibility that the toxin acted by increasing the permeability of membranes to ions was tested using a planar bilayer membrane system. Addition of the toxin to the bilayer system, under voltage-clamp conditions, resulted in stepwise increases in current across the phospholipid bilayer, a response characteristic for channel formers. Single-channel conductance in 1m KCl is 27 pS which corresponds to 1.7×107 ions sec−1 channel−1 at 100 mV applied potential. The toxin channels are: (i) fairly uniform in conductance, (ii) ideally selective for K+ over Cl−, and (iii) most conductive to H+. The channel showed the following selectivity for alkali metal cations: Rb+〉K+〉Cs+〉Na+〉Li+ (16∶9∶7∶3∶1) based on the most frequently observed conductance in 1m chloride salts. The toxin showed no voltage dependence over the range of −100 to +100 mV. Channel formation was also a property of a synthetic analog (Cmpd IV) of the toxin. The ability of the native toxin to form channels may be a mode of toxin action on mitochondrial membranes from susceptible corn.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01870661
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  • 10
    Electronic Resource
    Electronic Resource
    Patch clamping VDAC in liposomes containing whole mitochondrial membranes (1991)
    Springer
    The journal of membrane biology 123 (1991), S. 83-91 
    Details
    ISSN: 1432-1424
    Keywords: ion channels ; mitochondrial membranes ; voltage dependence ; VDAC ; Neurospora crassa
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Whole mitochondrial membranes isolated fromNeurospora crassa were reconstituted into liposomes and patch clamped. Clear activity characteristic of the mitochondrial channel VDAC was found, namely: open state conductance of 650 pS (in 150mm KCl, 1mm CaCl2, 20mm HEPES, pH 7.2), voltage-dependent closure at both positive and negative potentials, change in conductance upon channel closure of about 450 pS in response to negative and positive potentials, and increased voltage dependence in the presence of König's polyanion. This is the first clear demonstration of VDAC single channels using the patch-clamp technique, even though others used this method before to study whole mitochondrial membranes and liposomes containing mitochondrial proteins. We also found one other channel with a conductance change of about 120 pS.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01993966
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