These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: Reconstitution of Micrococcus lysodeikticus reduced nicotinamide adenine dinucleotide and L-malate dehydrogenases with dehydrogenase-depleted membrane residues: a basis for restoration of oxidase activities. Author: Eisenberg RC. Journal: J Bacteriol; 1972 Oct; 112(1):445-52. PubMed ID: 4342817. Abstract: Deoxycholate disruption of Micrococcus lysodeikticus protoplast membranes resulted in solubilization of both l-malate and reduced nicotinamide adenine dinucleotide (NADH) dehydrogenase enzymes (substrate: 2,6-dichlorophenolindophenol oxidoreductases). Insoluble residues contained cytochromes of the b, c, and a type. Solubilized dehydrogenases were reconstituted with insoluble residues by treatment of disrupted membranes with magnesium ions. Most of the solubilized l-malate and NADH dehydrogenase activities were precipitated by magnesium ions independent of enzyme reconstitution with insoluble residues. Reconstituted dehydrogenases explained the mechanism for restoration of disrupted l-malate and NADH oxidase activities (4). Black light irradiation inhibited oxidase activities of both native and reconstituted membranes. These irradiated membrane oxidases were partially restored by exogenous napthoquinones [K(2(20)) and K(2(50))] but not by CoQ((6)). Reconstitution experiments showed that native membrane napthoquinone was retained in the insoluble residues of deoxycholate-disrupted membranes.[Abstract] [Full Text] [Related] [New Search]