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Modulation of O 2 reduction in Saccharomyces cerevisiae mitochondria
Author(s) -
Rydström Lundin Camilla,
Brzezinski Peter
Publication year - 2017
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 - 10.1002/1873-3468.12918
Subject(s) - mitochondrion , saccharomyces cerevisiae , cytochrome c oxidase , cyanide , chemistry , biochemistry , potassium cyanide , heme , cytochrome c , oxidase test , respiratory chain , yeast , enzyme , inorganic chemistry
Respiratory supercomplex factor (Rcf) 1 is a membrane‐bound protein that modulates the activity of cytochrome c oxidase (Cyt c O) in Saccharomyces cerevisiae mitochondria. To investigate this regulatory mechanism, we studied the interactions of Cyt c O with potassium cyanide ( KCN ) upon removal of Rcf1. While the addition of KCN to the wild‐type mitochondria results in a full reduction of heme a , with the rcf1 Δ mitochondria, a significant fraction remains oxidized. Upon addition of ascorbate in the presence of O 2 and KCN , the reduction level of hemes a and b was a factor of ~ 2 larger with the wild‐type than with the rcf1 Δ mitochondria. These data indicate that turnover of Cyt c O was less blocked in rcf1 Δ than in the wild‐type mitochondria, suggesting that Rcf1 modulates the structure of the catalytic site.