Journal of the Spectroscopical Society of Japan

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Cytochrome c₁ shows an absorption spectrum very similar to that of cytochrome c and is confirmed to have haematohaem which is identical with the haem from cytochrome c.However, the absorption spectrum of cytochrome c₁ is not altered by the presence of CO, KCN or NaN₃ which brings about some change of the peaks in the case of cytochrome c.Therefore, the difference in physiological properties between these two components of cytochrome seems attributable to some difference in the nature of protein moiety, but the difference in linkage between haem moiety and protein moiety should probably be regarded also as involved.
No change in the absorption peaks of cytochrome c occurs even when cytochrome c is modified to a considerable extent.The change of its absorption spectrum on reduction and oxidation accompanies a considerable change in its property as protein;e.g.the reduced form of cytochrome c is not digested by bacterial proteinase, but its oxidized form easily digested.
P (Pseudomonas)-cytochrome₅₅₁, the absorption spectrum of which is very similar to that of cytochrome c, is found to differ from the latter inbehaviour against P-cytochrome oxidase.The reduced form of P-cytochrome₅₅₁ is oxidized by oxygen in the presence of the oxidase but not that of cytochrome c.
α-Absorption peak of cytochrome c is found to shift to 554 mμ in the presence of guanidine · HCI, and the same change occurs when cytochrome c is heated in a boiling water bath, but in the latter case the a-band reverts from 554 mμ to the original place, 550 mμ, by cooling.

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Details of a light source and an exitation assembly for Raman spectroscopy are reported.A Trontostyle mercury arc lamp is used.An electric circuit and accessories are designed so as to maintain the constant current operation of the arc and to minimize manual procedures for starting the arc.Safety devices are provided for the protection of the equipment in the event of failure of components or in fanlty.onperation.

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