A new low-spin, high-potential, water-soluble b-type cytochrome was is
olated from whitefish egg yolk. The cytochrome is termed b(560) accord
ing to the alpha-maximum in its difference (reduced-minus-oxidized) ab
sorption spectra. The absolute absorption spectrum of the reduced cyto
chrome measured at 20 degrees C has three characteristic maxima at 426
, 529, and 561 nm At 20 degrees C the oxidized form of the cytochrome
has a maximum in its gamma-spectral region at 416 nm. The difference s
pectrum of the cytochrome (reduced-minus-oxidized) has three character
istic maxima at 428, 529, and 560 nm. The midpoint redox potential of
the cytochrome is +193 mV and its molecular weight is 20.4 kD as indic
ated by electrophoresis under denaturing conditions. The reduced cytoc
hrome binds neither CO nor CN- and is oxidized by oxygen and hydrogen
peroxide with oxidation half-times of 28 and 2.4 min, respectively The
oxidized cytochrome is not reduced by cytochrome c or NAD(P)H but can
be rapidly reduced by sodium ascorbate.