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Reduction of exogenous cytochrome c by Neurospora crassa conidia: effects of superoxide dismutase and blue light

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The reduction of externally added cytochrome c by Neurospora crassa conidia was observed. The reduction was stimulated by antimycin A and suppressed partially by superoxide dismutase. When conidia were treated with diethyldithiocarbamate, which inactivated endogenous superoxide dismutase, the cytochrome c reduction was stimulated. Blue light also stimulated the cytochrome c reduction. Azide, which inhibits photochemical reactions mediated by flavins, suppressed the blue light effect. Superoxide dismutase partially suppressed the cytochrome c reduction in the light. The results suggest that O2(-) participates in the cytochrome c reduction by conidia and the flavins or flavoproteins are candidates for the receptor pigment of blue light to stimulate the cytochrome c reduction. It was also suggested that the redox component(s), which could directly transfer its reducing equivalents to exogenous cytochrome c, was present at the surface of conidia.
Title: Reduction of exogenous cytochrome c by Neurospora crassa conidia: effects of superoxide dismutase and blue light
Description:
The reduction of externally added cytochrome c by Neurospora crassa conidia was observed.
The reduction was stimulated by antimycin A and suppressed partially by superoxide dismutase.
When conidia were treated with diethyldithiocarbamate, which inactivated endogenous superoxide dismutase, the cytochrome c reduction was stimulated.
Blue light also stimulated the cytochrome c reduction.
Azide, which inhibits photochemical reactions mediated by flavins, suppressed the blue light effect.
Superoxide dismutase partially suppressed the cytochrome c reduction in the light.
The results suggest that O2(-) participates in the cytochrome c reduction by conidia and the flavins or flavoproteins are candidates for the receptor pigment of blue light to stimulate the cytochrome c reduction.
It was also suggested that the redox component(s), which could directly transfer its reducing equivalents to exogenous cytochrome c, was present at the surface of conidia.

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