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The dependence on quinone specificity of terminal electron transport of bacteria

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Abstract

Bacterial quinones were extracted with pentane, and homologues or other quinones were reincorporated. In spite of the redox potential difference of 110 mV, menaquinone and demethylmenaquinone could replace each other in aerobic electron transport and fumarate respiration ofHaemophilus influenzae RAMC 18 Bensted andProteus mirabilis Harding & Nicholson. The enzymes involved may recognize the naphthoquinone structure and are not specific for menaquinone or demethylmenaquinone. Ubiquinone was not replaced in aerobic electron transport by naphthoquinones withPseudomonas fluorescens 28/5 Rhodes orAcinetobacter sp. 661/60 Mannheim, probably owing to the specificity for benzoquinones of the enzymes involved, since the redox potential difference between demethylmenaquinone and ubiquinone is only 76 mV.Haemophilus parainfluenzae 429 Pittman, which resembles aerobic bacteria with respect to the terminal electron transport system, could incorporate demethylmenaquinone or menaquinone. This organism seems to be defective in the synthesis of naphthoquinones but possesses the enzyme system for fumarate respiration.Haemophilus influenzae RAMC 18 Bensted, which produces only demethylmenaquinone, seems to be defective in synthesizing ubiquinone, but it also possesses the enzymes for a ubiquinonemediated aerobic respiration.

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  1. Staatliches Medizinaluntersuchungsamt, Alte Poststrasse 11, D-4500, Osnabrück, Federal Republic of Germany

    Reinhard Holländer

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  1. Reinhard Holländer
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Holländer, R. The dependence on quinone specificity of terminal electron transport of bacteria. Current Microbiology 6, 155–159 (1981). https://doi.org/10.1007/BF01642390

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