The function of cytochrome c oxidase as a biomolecular nanomachine that transforms energy of redox reaction into protonmotive force across a biological membrane has been subject of intense research, debate, and controversy. The structure of the enzyme has been solved for several organisms; however details of its molecular mechanism of proton pumping still remain elusive. Particularly, the identity of the proton pumping site, the key element of the mechanism, is still open to dispute. The pumping mechanism has been for a long time one of the key unsolved issues of bioenergetics and biochemistry, but with the accelerating progress in this field many important details and principles have emerged. Current advances in cytochrome oxidase research are reviewed here, along with a brief discussion of the most complete proton pumping mechanism proposed to date, and a molecular basis for control of its efficiency.
Keywords:
Cytochrome c oxidase / Proton pumping mechanism / Kinetic control / Proton-coupled electron transfer / Catalytic cycle / Bioenergetics / Redox-driven proton pump
TY - JOUR
AU - Popović, Dragan
PY - 2013
UR - https://cer.ihtm.bg.ac.rs/handle/123456789/1195
AB - The function of cytochrome c oxidase as a biomolecular nanomachine that transforms energy of redox reaction into protonmotive force across a biological membrane has been subject of intense research, debate, and controversy. The structure of the enzyme has been solved for several organisms; however details of its molecular mechanism of proton pumping still remain elusive. Particularly, the identity of the proton pumping site, the key element of the mechanism, is still open to dispute. The pumping mechanism has been for a long time one of the key unsolved issues of bioenergetics and biochemistry, but with the accelerating progress in this field many important details and principles have emerged. Current advances in cytochrome oxidase research are reviewed here, along with a brief discussion of the most complete proton pumping mechanism proposed to date, and a molecular basis for control of its efficiency.
PB - Springer Wien, Wien
T2 - Amino Acids
T1 - Current advances in research of cytochrome c oxidase
VL - 45
IS - 5
SP - 1073
EP - 1087
DO - 10.1007/s00726-013-1585-y
UR - Conv_3046
ER -
@article{
author = "Popović, Dragan",
year = "2013",
abstract = "The function of cytochrome c oxidase as a biomolecular nanomachine that transforms energy of redox reaction into protonmotive force across a biological membrane has been subject of intense research, debate, and controversy. The structure of the enzyme has been solved for several organisms; however details of its molecular mechanism of proton pumping still remain elusive. Particularly, the identity of the proton pumping site, the key element of the mechanism, is still open to dispute. The pumping mechanism has been for a long time one of the key unsolved issues of bioenergetics and biochemistry, but with the accelerating progress in this field many important details and principles have emerged. Current advances in cytochrome oxidase research are reviewed here, along with a brief discussion of the most complete proton pumping mechanism proposed to date, and a molecular basis for control of its efficiency.",
publisher = "Springer Wien, Wien",
journal = "Amino Acids",
title = "Current advances in research of cytochrome c oxidase",
volume = "45",
number = "5",
pages = "1073-1087",
doi = "10.1007/s00726-013-1585-y",
url = "Conv_3046"
}
Popović, D.. (2013). Current advances in research of cytochrome c oxidase. in Amino Acids
Springer Wien, Wien., 45(5), 1073-1087.
https://doi.org/10.1007/s00726-013-1585-y
Conv_3046
Popović D. Current advances in research of cytochrome c oxidase. in Amino Acids. 2013;45(5):1073-1087.
doi:10.1007/s00726-013-1585-y
Conv_3046 .
Popović, Dragan, "Current advances in research of cytochrome c oxidase" in Amino Acids, 45, no. 5 (2013):1073-1087,
https://doi.org/10.1007/s00726-013-1585-y .,
Conv_3046 .
