Oxidation of c-Type Cytochromes by the Membrane-Bound Cytochrome Oxidase (Cytochrome aa(3)) of Blue-Green Algae.
نویسندگان
چکیده
Respiratory particles containing an aa(3)-type cytochrome oxidase were prepared from Anacystis nidulans, Synechocystis 6714, Synechococcus lividus, Anabaena variabilis, Nostoc sp. strain MAC, Nostoc muscorum, and Mastigocladus laminosus. Oxidation of c-type cytochromes by membrane preparations of the different blue-green algae was observed using purified cytochromes from horse heart, Candida krusei, tuna, Saccharomyces oviformis, Rhodospirillum rubrum, Rhodospirillum molischianum, Rhodopseudomonas palustris, Rhodocyclus purpureus, Paracoccus denitrificans, Anacystis nidulans, Anabaena variabilis, Euglena gracilis, and Scenedesmus obliquus. Rapid oxidations were consistently observed with the mitochondrial c-type cytochromes (horse heart cytochrome c reacts most rapidly) and with cytochromes c(2) from Rhodopseudomonas palustris and Rhodocyclus purpureus; in contrast, the cytochrome c(2) from Rhodospirillum rubrum and the plastidic cytochromes from E. gracilis and Scendesmus obliquus were inactive with all membrane preparations. All reactions were inhibited by low concentrations of KCN, NaN(3), and CO, and they were activated by Tween 80, thus indicating participation of the terminal oxidase. The results are discussed in view of the spectral similarities between the terminal oxidase of blue-green algae and the mitochondrial aa(3)-type cytochrome oxidase of plants and other eukaryotes.
منابع مشابه
Cytochrome Oxidase Activity in Cell-free Preparations from Blue-Green Algae.
The chlorophyll-containing lamellar structures isolated from Anabaena variabilis have the ability to oxidize reduced mammalian cytochrome c in the dark. This activity is oxygen dependent and heat labile. As with other cytochrome oxidase preparations, activity is stimulated by detergents and is sensitive to the ionic strength of the assay solution. The cytochrome oxidase activity is not inhibite...
متن کاملPhotosynthetic electron transport in a cell-free preparation from the thermophilic blue-green alga Phormidium laminosum.
1. A cell-free preparation of membrane fragments was prepared from the thermophilic blue-green alga Phormidium laminosum by lysozyme treatment of the cells followed by osmotic shock to lyse the spheroplasts. The membrane fragments showed high rates of photosynthetic electron transport and O2 evolution (180-250 mumol of O2/h per mg of chlorophyll a with 2,6-dimethyl-1,4-benzoquinone as electron ...
متن کاملProton pump coupled to cytochrome c oxidase in the cyanobacterium Anacystis nidulans.
Intact spheroplasts of the cyanobacterium Anacystis nidulans were found to oxidize various exogenous c-type cytochromes with concomitant proton extrusion. In the coupled state, H+/e stoichiometries close to 1 were measured, regardless of absolute reaction rates. It is concluded that the proton translocation observed is an intrinsic property of the cytoplasmic membrane-bound cytochrome c oxidase...
متن کاملCytochrome aa(3) in Haloferax volcanii.
A cytochrome in an extremely halophilic archaeon, Haloferax volcanii, was purified to homogeneity. This protein displayed a redox difference spectrum that is characteristic of a-type cytochromes and a CN(-) complex spectrum that indicates the presence of heme a and heme a(3). This cytochrome aa(3) consisted of 44- and 35-kDa subunits. The amino acid sequence of the 44-kDa subunit was similar to...
متن کاملSoluble CuA domain of cyanobacterial cytochrome c oxidase.
The genomes of several cyanobacteria show the existence of gene clusters encoding subunits I, II, and III of aa(3)-type cytochrome c oxidase. The enzyme occurs on both plasma and thylakoid membranes of these oxygenic phototrophic prokaryotes. Here we report the expression and purification of a truncated subunit II copper A (Cu(A)) domain (i.e. the electron entry and donor binding site) of cytoc...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Plant physiology
دوره 69 3 شماره
صفحات -
تاریخ انتشار 1982