Whole cells of the methylotrophic bacteriumMethylophilus methylotrophus cultured under methanol-limited conditions contain approximately equal amounts of two majorc-type cytochromes,c H andc L. Virtually all of the cytochromec H, and over one-third of the cytochromec L, are loosely attached to the periplasmic surface of the respiratory membrane whence they can be released by sonication or by washing cells in ethylenediaminetetraacetate (EDTA). The latter causes inhibition of methanol oxidase activity and stimulation of ascorbate-N,N,N′,N′-tetramethyl-p-phenylenediamine (TMPD) oxidase activity, neither of which effects are reversible by divalent metal ions. Kinetic analyses indicate that ascorbate-TMPD is oxidised via two routes, viz. a slow low-affinity pathway involving loosely membrane-boundc-type cytochromes plus cytochrome oxidaseaa 3, and a faster higher-affinity pathway involving the firmly membrane-bound cytochrome oxidasec L o complex; the former route predominates in the presence of divalent metal ions, and the latter route after exposure to EDTA. These and other results are discussed in terms of the spatial organisation of the terminal respiratory chain, and of the role ofc-type cytochromes in the oxidation of methanol and ascorbate-TMPD.
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Concentration of inhibitor required to give 50% inhibition of enzyme activity
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Carver, M.A., Jones, C.W. The role ofc-type cytochromes in the terminal respiratory chain of the methylotrophic bacteriumMethylophilus methylotrophus . Arch. Microbiol. 139, 76–82 (1984). https://doi.org/10.1007/BF00692716
- Bacterial respiration
- Methylophilus methylotrophus
- Respiratory membrane