TY  - JOUR
A1  - Harrenga, Axel
A1  - Michel, Hartmut
T1  - The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction
T2  - Journal of biological chemistry
N2  - Cytochrome c oxidase catalyzes the reduction of oxygen to water. This process is accompanied by the vectorial transport of protons across the mitochondrial or bacterial membrane (“proton pumping”). The mechanism of proton pumping is still a matter of debate. Many proposed mechanisms require structural changes during the reaction cycle of cytochrome c oxidase. Therefore, the structure of the cytochrome c oxidase was determined in the completely oxidized and in the completely reduced states at a temperature of 100 K. No ligand exchanges or other major structural changes upon reduction of the cytochrome coxidase from Paracoccus denitrificans were observed. The three histidine CuB ligands are well defined in the oxidized and in the reduced states. These results are hardly compatible with the “histidine cycle” mechanisms formulated previously.
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/75864
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-758640
SN  - 0021-9258
VL  - 274
IS  - 47
SP  - 33296
EP  - 33299
PB  - American Society for Biochemistry and Molecular Biology Publications
CY  - Bethesda, Md
ER  -