Indications for the occurrence of nitric oxide synthases in Dictyostelium, Neurospora, Phycomyces and the leguminous plant Mucuna hassjoo as well as a physiological role of nitric oxide in Neurospora crassa are demonstrated. An exogenous nitic oxide donor, sodium nitroprusside, inhibited light-stimulated conidiation in N. crassa. Specific inhibitors of nitric oxide synthase, like the arginine derivatives NG -nitro-L-arginine (L-NA) and NG-nitro-L-arginine-methyl ester (L-NAME), enhanced conidiation in darkness nad in the light, whereas the stereoisomer D-NAME was inactive. This communication reports to our knowledge the first time the presence of enzymatic activity of nitric oxide synthase in fungi and a higher plant and an effect of nitric oxide in fungal photo-physiology.

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Blue light controls the development of sporangiophores in the zygomycete Phycomyces blakesleeanus Burgeff. Light represses the production of microsporangiophores and enhances the development of macrosporangiophores. Inhibition of the biosynthesis of tetrahydrobiopterin, a cofactor of NO synthase, inhibits this photomorphogenesis. Light induces production of citrulline from arginine in the mycelium and in sporangiophores. The citrulline-forming activity is dependent on NADPH, independent of calcium, and inhibited by NO synthase inhibitors. It is reduced in tetrahydrobiopterin-depleted mycelium. Light induces emission of NO from the developing fungus in the same order of magnitude as citrulline formation from arginine. The NO donor sodium nitroprusside can replace the light effect on sporangiophore development, and inhibitors of NO synthase repress it. We suggest that a fungal NO synthase is involved in sporangiophore development and propose its participation in light signaling.

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Occurrence, biosynthesis and some functions of tetrahydrobiopterin (H4biopterin) in animals are well known. The biochemistry of H4biopterin in other organisms than animals was hitherto not widely investigated. Recently H4biopterin was found in the phytoflagellate Euglena gracilis, in the zygomycete Phycomyces blakesleeanus and in the ascomycete Neurospora crassa. In Euglena, Neurospora and Phycomyces the enzymatic activities of GTP cyclohydrolase I, 6-pyruvoyl tetrahydropterin synthase and sepiapterin reductase are detectable and the biosynthesis follows the same steps as were shown for animals. The biosynthetic enzymes, however, show a much lower sensitivity to those inhibitors that act on vertebrate enzymes. 2,4-Diamino-6-hydroxypyrimidine as inhibitor of GTP cyclohydrolase I and N-acetylserotonin or N-methoxyacetylserotonin as inhibitors of sepiapterin reductase can decrease pteridine biosynthesis significantly, in vitro and in vivo. The apparent Km values are in general higher when compared with the respective animal enzymes. In Neurospora, the conversion of GTP to dihydroneopterin triphosphate was closely associated with subsequent production of 6-hydroxymethyl-7,8-dihydropterin due to the high activity of dihydroneopterin aldolase, different from all other tested organisms. Investigations involving inhibition of pteridine synthesis might be a useful tool for evaluating the hypothesis that pteridines in fungi and plants are co-chromophores of various blue light-dependent, flavin-containing photoreceptors.

The light-harvesting Chl-aib protein complex (LHC) of Lactuca saticu L. was examined for pigment content, excitation energy transfer and behavior under acidic conditions:(1) Lettuce LHC contains Chl-a, Chl-b and xanthophylls (lutein, neoxanthin, lactucaxanthin, violaxanthin) at a molar ratio of 6:4:3; their contribution to the absorbance of the LHC between 390 and 530 nm is estimated to be about 31% (Chl-a), 26% (Chl-b) and 43% (xanthophylls). 12) Energy transfer from xanthophylls and Chl-b to Chl-a takes place at 100% transfer efficiency.(3) LHC exhibits an unusual acid stability: in contrast to complexes of photosystem I or 11, LHCbound chlorophylls are not converted to phaeophytin and LHC apoprotein is not denatured at pH 1.5; also. energy transfer is maintained.(4) Pronase or trypsin treatment do not affect acid stability and energy transfer.( 5 ) Treatments that break down acid stability (heat, urea or Triton X-100) also inhibit energy transfer.The coincidental breakdown of energy transfer and acid stability points at one underlying process, namely. the breakdown of a structure that enables protection of chlorophylls from proton attack and close contiguity of xanthophylls and chlorophylls as required for energy transfer. Dense packing of xanthophylls and chlorophylls within lipophilic crevices of the LHC is suggested.

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