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Kinetic limitations in the overall reaction of mitochondrial oxidative phosphorylation accounting for flux‐dependent changes in the apparent Δ G ex P /Δ H + ratio
Author(s) -
Kunz Wolfgang,
Gellerich Frank Norbert,
Schild Lorenz,
Schönfeld Peter
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)81347-4
Subject(s) - oxidative phosphorylation , chemistry , adenine nucleotide translocator , flux (metallurgy) , kinetics , atpase , biophysics , biochemistry , physics , biology , enzyme , organic chemistry , quantum mechanics
Changes in J 0 , Δ H + and Δ G ex P were investigated as a function of load. The flux control coefficients, particularly those of the adenine nucleotide translocator and H + ‐ATPase at the maximum rate of oxidative phosphorylation were seen to strongly depend on the phosphate concentration accounting in common for the highest share in flux control. There was no unique relationship observed between J P and Δ H + in load‐controlled, well coupled systems, but J P was found to depend on Δ H + at excessive load and increasing proton leakage. All the results presented can be elucidated on the grounds of delocalized chemiosmotic coupling.