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Chlorella vulgaris structure

Chlorella vulgaris nitrate reductase structure, 3,1438 Chlorides... [Pg.100]

Shigeoka, T., Sato, Y., Takeda, Y. (1988) Acute toxicity of chlorophenols to green algae, Selenastrum capricomutum and Chlorella vulgaris, and quantitative structure-activity relationships. Environ. Toxicol. Chem. 7, 847-854. [Pg.57]

Both assimilatory and dissimilatory nitrate reductases are molybdoenzymes, which bind nitrate at the molybdenum. EXAFS studies1050 have shown that there are structural differences between the assimilatory nitrate reductase from Chlorella vulgaris and the dissimilatory enzyme from E. coli. The Chlorella enzyme strongly resembles sulfite oxidase1050,1053 and shuttles between mon-and di-oxo forms, suggesting an oxo-transfer mechanism for reduction of nitrate. This does not appear to be the case for the E. coli enzyme, for which an oxo-transfer mechanism seems to be unlikely. The E. coli enzyme probably involves an electron transfer and protonation mechanism for the reduction of nitrate.1056 It is noteworthy that the EXAFS study on the E. coli nitrate reductase showed a long-distance interaction with what could be an electron-transfer subunit. [Pg.725]

Cerium tetrakis(acetylacetonate), 1114 Cesium complexes crown ethers, 40 Chevrel phases, 1321 Chlorella vulgaris nitrate reductase structure, 1438 Chlorine cations... [Pg.3290]


See other pages where Chlorella vulgaris structure is mentioned: [Pg.179]    [Pg.179]    [Pg.467]    [Pg.67]    [Pg.164]    [Pg.367]    [Pg.398]    [Pg.540]    [Pg.94]   
See also in sourсe #XX -- [ Pg.1438 ]

See also in sourсe #XX -- [ Pg.3 , Pg.1438 ]




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Chlorella

Chlorella vulgaris

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