Abstract
Pseudomonas cytochrome oxidase (ferrocytochrome c2:O2 oxido-reductase, EC 1.9.3.2) functions as a terminal electron carrier in the bacterium Pseudomonas aeruginosa. The oxidase can donate electrons either to molecular oxygen or to nitrite although it appears that in situ it is intended to react with nitrite rather than 02 since the enzyme is only synthesized when the organism is grown anaerobically in the presence of nitrate or nitrite. However, since Pseudomonas cytochrome oxidase can catalyze the reduction of O2 to H2O (a four-electron transfer) it bears some similarity functionally to the cytochrome c oxidase of the mitochondrial respiratory chain.
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© 1976 Plenum Press, New York
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Wharton, D.C., Hill, K., Gibson, Q.H. (1976). Heme Interactions in Pseudomonas Cytochrome Oxidase. In: Yasunodu, K.T., Mower, H.F., Hayaishi, O. (eds) Iron and Copper Proteins. Advances in Experimental Medicine and Biology, vol 74. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3270-1_17
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DOI: https://doi.org/10.1007/978-1-4684-3270-1_17
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