Identification of the site where the electron transfer chain of plant mitochondria is stimulated by electrostatic charge screening.

K. Krab; M.J. Wagner; A.M. Wagner; I.M. Moller

doi:10.1046/j.1432-1327.2000.01065.x

Identification of the site where the electron transfer chain of plant mitochondria is stimulated by electrostatic charge screening.

K. Krab, M.J. Wagner, A.M. Wagner, I.M. Moller

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

Modular kinetic analysis was used to determine the sites in plant mitochondria where charge-screening stimulates the rate of electron transfer from external NAD(P)H to oxygen. In mitochondria isolated from potato (Solanum tuberosum L.) tuber callus, stimulation of the rate of oxygen uptake was accompanied by a decrease in the steady-state reduction level of coenzyme Q, and by a small decrease in the steady-state reduction level of cytochrome c. Modular kinetic analysis around coenzyme Q revealed that stimulation of the rate was due to stimulation of quinol oxidation via the cytochrome pathway (cytochrome bc

Original language	English
Pages (from-to)	869-876
Number of pages	8
Journal	European Journal of Biochemistry
Volume	267
DOIs	https://doi.org/10.1046/j.1432-1327.2000.01065.x
Publication status	Published - 2000

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title = "Identification of the site where the electron transfer chain of plant mitochondria is stimulated by electrostatic charge screening.",

abstract = "Modular kinetic analysis was used to determine the sites in plant mitochondria where charge-screening stimulates the rate of electron transfer from external NAD(P)H to oxygen. In mitochondria isolated from potato (Solanum tuberosum L.) tuber callus, stimulation of the rate of oxygen uptake was accompanied by a decrease in the steady-state reduction level of coenzyme Q, and by a small decrease in the steady-state reduction level of cytochrome c. Modular kinetic analysis around coenzyme Q revealed that stimulation of the rate was due to stimulation of quinol oxidation via the cytochrome pathway (cytochrome bc",

author = "K. Krab and M.J. Wagner and A.M. Wagner and I.M. Moller",

year = "2000",

doi = "10.1046/j.1432-1327.2000.01065.x",

language = "English",

volume = "267",

pages = "869--876",

journal = "European Journal of Biochemistry",

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T1 - Identification of the site where the electron transfer chain of plant mitochondria is stimulated by electrostatic charge screening.

AU - Krab, K.

AU - Wagner, M.J.

AU - Wagner, A.M.

AU - Moller, I.M.

PY - 2000

Y1 - 2000

N2 - Modular kinetic analysis was used to determine the sites in plant mitochondria where charge-screening stimulates the rate of electron transfer from external NAD(P)H to oxygen. In mitochondria isolated from potato (Solanum tuberosum L.) tuber callus, stimulation of the rate of oxygen uptake was accompanied by a decrease in the steady-state reduction level of coenzyme Q, and by a small decrease in the steady-state reduction level of cytochrome c. Modular kinetic analysis around coenzyme Q revealed that stimulation of the rate was due to stimulation of quinol oxidation via the cytochrome pathway (cytochrome bc

AB - Modular kinetic analysis was used to determine the sites in plant mitochondria where charge-screening stimulates the rate of electron transfer from external NAD(P)H to oxygen. In mitochondria isolated from potato (Solanum tuberosum L.) tuber callus, stimulation of the rate of oxygen uptake was accompanied by a decrease in the steady-state reduction level of coenzyme Q, and by a small decrease in the steady-state reduction level of cytochrome c. Modular kinetic analysis around coenzyme Q revealed that stimulation of the rate was due to stimulation of quinol oxidation via the cytochrome pathway (cytochrome bc

U2 - 10.1046/j.1432-1327.2000.01065.x

DO - 10.1046/j.1432-1327.2000.01065.x

M3 - Article

SN - 0014-2956

VL - 267

SP - 869

EP - 876

JO - European Journal of Biochemistry

JF - European Journal of Biochemistry

ER -

Identification of the site where the electron transfer chain of plant mitochondria is stimulated by electrostatic charge screening.

Abstract

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