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Respiratory activities and aa 3 type cytochrome oxidase in plasma and thylakoid membranes from vegetative cells and heterocysts of the cyanobacterium anabaena atcc 29413


Respiratory activities and aa 3 type cytochrome oxidase in plasma and thylakoid membranes from vegetative cells and heterocysts of the cyanobacterium anabaena atcc 29413



Biochimica et Biophysica Acta 935(2): 217-224



ISSN/ISBN: 0005-2728

DOI: 10.1016/0005-2728(88)90218-6

Plasma and thylakoid membranes were separated by discontinuous sucrose density gradient centrifugation from crude membrane preparations of vegetative cells and heterocysts of the nitrogen-fixing cyanobacterium Anabaena ATCC 29413. Isolated and purified plasma membranes were devoid of spectroscopically detectable chlorophyll. Intact heterocysts were separated from vegetative cells by selective lysozyme degradation of the latter, followed by low-pressure French-press extrusion and differential centrifugation. Each of the four types of membrane preparation oxidized horse heart ferrocytochrome c, rates ranging from 35 nmol/min per mg protein (plasma membrane from vegetative cells) to 2400 nmol/min per mg protein (thylakoid membranes from heterocysts). The reactions were stimulated up to 6-fold by 0.05% (w/v) n-octyl glucoside; they were completely inhibited by 1.2 .mu.M KCN and severely inhibited by CO. The cytochrome oxidase present in n-octylglugcoside-solubilized membranes could be enriched about 10-fold by affinity chromatography on immobilized yeast cytochrome c. Extraction with acidic butanone-2 or acetone, followed by preparation of the alkaline pyridine ferrohemochrome derivatives, proved the presence of a-type cytochrome. Sodium dodecylsulfate polyacrylamide gel electropherograms of the four membrane types were characteristically different from each other. Immunoblotting of the membrane polypeptides were antisera against the aa3-type cytochrome of Paracoccus denitrificans (subunits I and II and holoenzyme) and rat liver mitochodnria (subunit II) gave specific and complementary cross-reaction at about 48-49 and 36 kDa (subunits I and II, respectively) irrespective of the membranes used. In addition to oxidizing ferrocytochrome c, the isolated membranes were also found to reduce horse heart ferricytochrome c to variable extents with NAD(P)H.

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Accession: 006323189

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