A Manganese Protein from Thylakoids of a Cyanobacterium, Plectonema boryanum; Inhibition of Oxygen Evolution with Its Antibody
- 1 January 1983
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant and Cell Physiology
- Vol. 24 (2), 163-172
- https://doi.org/10.1093/pcp/24.2.163
Abstract
A manganese protein was solubilized from the thylakoids of the cyanobacterium Plectonema boryanum with a cholate-deoxycholate mixture, and purified to homogeneity by gel-filtration. Isolated manganese protein had a molecular weight of 13,000 and showed catalase activity, which was insensitive to 3-aminotriazole. The antibody raised against the manganese protein inhibited the oxygen evolution using dichlorophenol indophenol (DCIP) as the electron acceptor by P. boryanum thylakoids, but not the diphenylcarbazide-supported photoreduction of DCIP and ascorbate-supported photoreduction of methyl viologen in the presence of DCMU. These observations suggest that isolated manganese protein is a component of the oxygen evolving enzyme, water dehydrogenase.This publication has 4 references indexed in Scilit:
- Action of cyanide on the photosynthetic water-splitting processBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1982
- Inactivation of Photosynthetic Oxygen Evolution and Concomitant Release of Three Polypeptides in the Photosystem II Particles of Spinach ChloroplastsPlant and Cell Physiology, 1982
- Proton release in photosynthetic water oxidation: evidence for proton movement in a restricted domainBiochemistry, 1981
- 7 CatalasePublished by Elsevier ,1976