Abstract
The spectral properties of the cytochrome system of the sperm from two species of sea urchin, Lythechinus pictus and Strongylocentrolus purpuratus, were examined with the sperm samples at room temperature and at liquid nitrogen temperatures. The sperm contain cytochromes a, a 3, b, c, and c 1 in a ratio of 1:1:1:2:1 where 1 unit is 0.05 μmoles per gram protein. Antimycin A causes a shift in the alpha maximum of reduced cytochrome b from 560 to 565 mμ (25 °C) and an apparent increase in the concentration of substrate-reducible cytochrome b. Cyanide and sulfide inhibit respiration by interacting with oxidized cytochrome a 3 while carbon monoxide binds reduced cytochrome a 3. The carbon monoxide compound is photodissociable and the photochemical action spectrum from the carbon monoxide-inhibition of respiration has maxima at 587 mμ, 548 mμ, and 428 mμ. Azide inhibition of respiration occurs concomitant with a shift of the alpha maximum and split Soret maxima of reduced cytochrome a to shorter wavelengths and this shift is reversed by cyanide, carbon monoxide, and anaerobiosis.
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