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Pseudomonas perfectomarinus

Balderston, W. L., Sherr, B., and Payne, W. J. (1976). Blockage by acetylene of nitrous oxide reduction in Pseudomonas perfectomarinus. Appl. Environ. Microbiol. 31, 504-508. [Pg.330]

Zumft, W. G., and Frunzke, K. (1982). Discrimination of ascorbate-dependent nonenzy-matic and enzymatic, membrane-bound reduction of nitric oxide in denitrifying Pseudomonas perfectomarinus. Biochim. Biophys. Acta 681, 459-468. [Pg.344]

Figure 4. Two examples of the relationship between ETS activity and the oxygen-consumption rate in natural seawater samples (top) and in laboratory cultures of the marine bacterium Pseudomonas perfectomarinus (bottom). Figure 4. Two examples of the relationship between ETS activity and the oxygen-consumption rate in natural seawater samples (top) and in laboratory cultures of the marine bacterium Pseudomonas perfectomarinus (bottom).
A second proteinaceous fraction, nitric oxide reductase, containing a bound c-type cytochrome converts nitric oxide to nitrous oxide (Matsubara and Iwasaki, 1971 Payne et al., 1971 Cox and Payne, 1973). The enzyme is soluble in Pseudomonas perfectomarinus (Cox and Payne, 1973), but is particulate in Alcaligenes faecalis and Pseudomonas denitrificans (Matsubara and Iwasaki, 1971 Miyata et al., 1969). Epr studies indicate no metal involvement but the formation of a different heme nitric oxide complex during release of nitrous oxide (Payne et al., 1971). The physiological electron donors are not known. FADHa, reduced phenazine methosulphate, and reduced viologen dyes have been found to be effective (Thauer et al., 1977). [Pg.135]


See other pages where Pseudomonas perfectomarinus is mentioned: [Pg.190]    [Pg.152]    [Pg.190]    [Pg.152]   
See also in sourсe #XX -- [ Pg.135 ]

See also in sourсe #XX -- [ Pg.12 ]




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