Electron transport chain in Micrococcus lysodeikticus cytoplasmic membranes

Gel'man, N.S.; Lukoyanova, M.A.; Zhukova, I.G.; Oparin, A.I.

Biokhimiya 28(5): 801-807


Accession: 024602684

Download citation:  

Article/Abstract emailed within 1 workday
Payments are secure & encrypted
Powered by Stripe
Powered by PayPal

Succinate, malate and reduced form of diphosphopyridine-nucleotide (DPN-H) oxidation is accomplished by intact bacteria, lysed cells and cytoplasmic membranes via electron (H) transport chain which is common for all these substrates. The electron transfer is not inhibited by cyanide or antimycin-A. Malate oxidase and DPN-H dehydrogenase stability during the cell lysis is due to the fact that malate dehydrogenase and DPN-H dehydrogenase are firmly bound to the enzymes of the electron transport chain of the cytoplasmic membrane. Succinic dehydrogenase activity is decreased 90% by cell lysis due to a cleavage of bonds between succinic dehydrogenase or some unidentified factor with the enzymes of electron transport chain.