1966
DOI: 10.1093/oxfordjournals.jbchem.a128477
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Studies on Soluble Cytochromes in Enterobacteriaceae

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Cited by 37 publications
(9 citation statements)
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“…Cytochrome c552 is probably the inhibition site of cyanide and cupric ion in the system. Fujita and Sat0 found that cytochrome cs52 is located at the periplasmic space [8] and Jones et al observed nitrite reductase activity with viologen dyes as electron donor at the periplasmic side of the cytoplasmic membrane [26]. Considering the cellular location of cytochrome c 5 5 2 , electrons are probably not transferred from NADH to nitrite via soluble NADH oxidase, FAD, and cytochrome c552 [13].…”
Section: Discussionmentioning
confidence: 99%
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“…Cytochrome c552 is probably the inhibition site of cyanide and cupric ion in the system. Fujita and Sat0 found that cytochrome cs52 is located at the periplasmic space [8] and Jones et al observed nitrite reductase activity with viologen dyes as electron donor at the periplasmic side of the cytoplasmic membrane [26]. Considering the cellular location of cytochrome c 5 5 2 , electrons are probably not transferred from NADH to nitrite via soluble NADH oxidase, FAD, and cytochrome c552 [13].…”
Section: Discussionmentioning
confidence: 99%
“…In E. coli K12, this synthesis is under the control of an activator protein encoded by the j n r gene, which is necessary for the induced synthesis of a number of components in the anaerobic respiratory systems, including nitrate reductase, nitrite reductase, fumarate reductase, and hydrogenase [4] reported that reduced cytochrome c S s 2 from E. coli Yamaguchi is rapidly reoxidized by addition of nitrite. They found that cytochrome ~5 5 2 is located in the periplasinic space [8] and concluded that its in vivo function is reduction of toxic nitrite produced by nitrate respiration to ammonia at the cell surface 191. However, the protein-chemical properties of the cytochrome as a nitrite reductase have not been studied extensively.…”
mentioning
confidence: 99%
“…It contains 4-6 c haem molecules/SO-kDa subunit. Fujita (1966) and Sato (1966a, b, 1967) first identified a membrane-bound nitrite-reducing cytochrome c 5 s 2 in E. coli. The enzyme is part of an electron transfer chain for which formate has been shown to be the electron donor (Colc and Ward, 1973;Abou-Jaoude el al., 1979).…”
Section: Assimilatory and Dissimilatory Enzymesmentioning
confidence: 99%
“…2). Reduction of nitrite is assumed to take place at the periplasmic surface of the membrane because this is the location of cytochrome c552 [15] which is possibly either the nitrite reductase itself or alternatively the immediate donor of electrons to the nitrite reductase. When an initial 2Fmol was supplemented by a further 2/~mol, steady-state BTPP + uptake occurred.…”
Section: Decreased Membrane Potential With High Concentrations Of Nitmentioning
confidence: 99%