Cell Respiration is Controlled by ATP, an Allosteric Inhibitor of Cytochrome‐<i>c</i> Oxidase

10.1073/pnas.90.5.1652

10.1111/j.1432-1033.1997.t01-1-00099.x

10.1152/ajpcell.1984.246.1.C10

10.1152/ajpcell.1990.258.3.C377

10.1016/S0300-9084(85)80237-6

10.1016/0003-2697(76)90527-3

Brosnan M. J., 1990, Free ADP levels in transgenmic mouse liver expressing creatine kinase. Effects of enzyme activity, phosphagen type, and substrate concentration, J. Biol. Chern., 265, 20849, 10.1016/S0021-9258(17)45293-8

10.1111/j.1432-1033.1982.tb05882.x

Chance B., 1955, Respirtatory enzymes in oxidative phosphorylation. 111. The steady state, J. Biol. Chem., 217, 405, 10.1016/S0021-9258(19)57192-7

10.1042/bj2360359

10.1021/bi00008a036

10.1021/bi00005a009

Ferguson‐Miller S., 1976, Correlation of the kinetics of electron transfer activity of various eukaryotic cytochromes c with binding to mitochondrial cytochrome‐c oxidase, J. Biol. Chem., 251, 1104, 10.1016/S0021-9258(17)33807-3

Ferguson‐Miller S., 1978, Definition of cytochrome c binding domains by chemical modification. III. Kinetics of reaction of carboxydinitrophenyl cytochromes c with cytochrome‐c oxidase, J. Biol. Chem., 253, 149, 10.1016/S0021-9258(17)38281-9

10.1016/0014-5793(96)00096-8

10.1021/bi00467a020

10.1074/jbc.270.6.2466

10.1016/0005-2728(87)90112-5

10.1016/S0006-291X(87)80207-3

10.1038/376660a0

10.1016/0014-5793(82)80498-5

10.1016/0014-5793(87)80939-0

10.1152/ajpheart.1989.256.1.H265

10.1021/bi00303a009

Lardy H. A., 1952, Oxidative phosphorylation: role of inorganic phosphate and acceptor systems in control of metabolic rates, J. Biol. Chem., 195, 215, 10.1016/S0021-9258(19)50892-4

10.1111/j.1469-185X.1966.tb01501.x

10.1515/bchm.1997.378.9.1013

Nicholls D. G., 1992, Bioenergetics

10.1007/BF01108409

10.1042/bj2540723

10.1007/BF00762857

10.1111/j.1432-1033.1991.tb15989.x

Suarez M. D., 1984, The functional and physical form of mammalian cytochrome‐c oxidase determined by gel filtration, radioation inactivation, and sedimentation equilibrium analysis, J. Biol. Chem., 259, 13791, 10.1016/S0021-9258(18)89815-5

10.1126/science.7652554

10.1126/science.272.5265.1136

10.1016/S0021-9258(18)50401-4

10.1152/ajpcell.1993.265.2.C365

10.1152/ajpcell.1988.255.5.C581

10.1073/pnas.85.5.1354