Respiratory Chain of Colorless Algae II. Cyanophyta
Author(s) -
D.A. Webster,
David P. Hackett
Publication year - 1966
Publication title -
plant physiology
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.41.4.599
Subject(s) - oxidase test , algae , cytochrome c oxidase , respiration , cytochrome , pigment , biochemistry , biology , blue green algae , bacteria , enzyme , chemistry , botany , cyanobacteria , organic chemistry , genetics
Whole cell difference spectra of the blue-green algae, Saprospira grandis, Leucothrix mucor, and Vitreoscilla sp. have one, or at the most 2, broad alpha-bands near 560 mmu. At -190 degrees these bands split to give 4 peaks in the alpha-region for b and c-type cytochromes, but no alpha-band for a-type cytochromes is visible. The NADH oxidase activity of these organisms was shown to be associated with particulate fractions of cell homogenates. The response of this activity to inhibitors differed from the responses of the NADH oxidase activities of particulate preparations from the green algae and higher plants to the same inhibitors, but is more typical of certain bacteria. No cytochrome oxidase activity was present in these preparations. The respiration of Saprospira and Vitreoscilla can be light-reversibly inhibited by CO, and all 3 organisms have a CO-binding pigment whose CO complex absorbs near 570, 535, and 417 mmu. The action spectrum for the light reversal of CO-inhibited Vitreoscilla respiration shows maxima at 568, 534, and 416 mmu. The results suggest that the terminal oxidase in these blue-greens is an o-type cytochrome.
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