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Identification of a copper protein as part of the nitrous oxide-reducing system in nitrite-respiring (denitrifying) pseudomonads

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Abstract

Copper is the essential transition element for nitrous oxide respiration in Pseudomonas perfectomarinus. Two novel kinds of copper proteins were detected in this organism. Their distribution was studied under different growth conditions and in other pseudomonads, as well as their association with N2O reduction of intact cells. A low molecular mass copper protein (M r 38,000) with a single absorption band at 340 nm (oxidized form), was found only in P. perfectomarinus and was not required for N2O reduction. N2O respiration was consistently associated with a high molecular mass copper protein (M r 120,000) in P. perfectomarinus, Pseudomonas stutzeri, and in strains of Pseudomonas fluorescens that were capable of this type of respiration. The oxidized protein was violet to pink with absorption bands at 350, 480, 530, 620, and 780 nm. Pseudomonas chlororaphis and Pseudomonas aureofaciens which did not respire with N2O as electron acceptor, did not contain the novel type of copper protein. Cytochrome patterns were compared in these denitrifying pseudomonads to search for the physiological electron carrier to N2O reductase. The content and nature of the soluble c-type cytochromes depended strongly on the species and the particular growth condition.

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Abbreviations

M r :

relative molecular mass

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Matsubara, T., Zumft, W.G. Identification of a copper protein as part of the nitrous oxide-reducing system in nitrite-respiring (denitrifying) pseudomonads. Arch. Microbiol. 132, 322–328 (1982). https://doi.org/10.1007/BF00413383

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  • DOI: https://doi.org/10.1007/BF00413383

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