The role of the D- and K-pathways of proton transfer in the function of the haem-copper oxidases.
The X-ray structures of several haem-copper oxidases now at hand have given important constraints on how these enzymes function. Yet, dynamic data are required to elucidate the mechanisms of electron and proton transfer, the activation of O(2) and its reduction to water, as well as the still enigmatic mechanism by which these enzymes couple the redox reaction to proton translocation. Here, some recent observations will be briefly reviewed with special emphasis on the functioning of the so-called D- and K-pathways of proton transfer. It turns out that only one of the eight protons taken up by the enzyme during its catalytic cycle is transferred via the K-pathway. The D-pathway is probably responsible for the transfer of all other protons, including the four that are pumped across the membrane. The unique K-pathway proton may be specifically required to aid O-O bond scission by the haem-copper oxidases.
Wikström
M
M
Department of Medical Chemistry, Institute of Biomedical Sciences and Biocentrum Helsinki, University of Helsinki, Finland. marten.wikstrom@helsinki.fi
Jasaitis
A
A
Backgren
C
C
Puustinen
A
A
Verkhovsky
M I
MI
D001665:Binding Sites; D006418:Heme / Q000031:analogs & derivatives / Q000737:chemistry*; D007700:Kinetics; D008024:Ligands; D008956:Models, Chemical; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry*; D010231:Paracoccus denitrificans; D017494:Proton Pumps / Q000737:chemistry; D011522:Protons
D008024:Ligands; D017494:Proton Pumps; D011522:Protons; D006418:Heme; D010088:Oxidoreductases; C024748:copper oxidase