New insights in the regulation of the plant succinate dehydrogenase - on the role of the protonmotive force.

C. Affourtit; K. Krab; G.R. Leach; D.G. Whitehouse; A.L. Moore

doi:10.1074/jbc.M103111200

New insights in the regulation of the plant succinate dehydrogenase - on the role of the protonmotive force.

C. Affourtit
, K. Krab
, G.R. Leach
, D.G. Whitehouse
, A.L. Moore

Biophysics Photosynthesis/Energy

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

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Abstract

Regulation of succinate dehydrogenase was investigated using tightly coupled potato tuber mitochondria in a novel fashion by simultaneously measuring the oxygen uptake rate and the ubiquinone (Q) reduction level. We found that the activation level of the enzyme is unambiguously reflected by the kinetic dependence of the succinate oxidation rate upon the Q-redox poise. Kinetic results indicated that succinate dehydrogenase is activated by both ATP (K

Original language	English
Pages (from-to)	32567-32574
Journal	Journal of Biological Chemistry
Volume	276
DOIs	https://doi.org/10.1074/jbc.M103111200
Publication status	Published - 2001

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title = "New insights in the regulation of the plant succinate dehydrogenase - on the role of the protonmotive force.",

abstract = "Regulation of succinate dehydrogenase was investigated using tightly coupled potato tuber mitochondria in a novel fashion by simultaneously measuring the oxygen uptake rate and the ubiquinone (Q) reduction level. We found that the activation level of the enzyme is unambiguously reflected by the kinetic dependence of the succinate oxidation rate upon the Q-redox poise. Kinetic results indicated that succinate dehydrogenase is activated by both ATP (K",

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AU - Whitehouse, D.G.

AU - Moore, A.L.

PY - 2001

Y1 - 2001

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AB - Regulation of succinate dehydrogenase was investigated using tightly coupled potato tuber mitochondria in a novel fashion by simultaneously measuring the oxygen uptake rate and the ubiquinone (Q) reduction level. We found that the activation level of the enzyme is unambiguously reflected by the kinetic dependence of the succinate oxidation rate upon the Q-redox poise. Kinetic results indicated that succinate dehydrogenase is activated by both ATP (K

U2 - 10.1074/jbc.M103111200

DO - 10.1074/jbc.M103111200

M3 - Article

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SP - 32567

EP - 32574

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

ER -

New insights in the regulation of the plant succinate dehydrogenase - on the role of the protonmotive force.

Abstract

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