The aim of this work was to determine the extent to which the periplasmic cytochromes and blue copper proteins could replace each other during growth of an obligate methylotroph (organism 4025) on methanol and methylamine. This was done by varying the relative concentrations of these proteins as a result of varying the amount of copper added to the growth medium during growth in oxygen-limited conditions. It was shown that the amount of added copper required for maximum growth was greater during growth on methylamine than on methanol. The concentrations of membrane-bound cytochromes b, c and o were not markedly affected by the copper concentration added to the growth medium whereas the concentrations of soluble cytochromes and blue copper proteins varied considerably. The concentrations of cytochrome cL were highest at the copper concentrations giving maximum growth; this was more obvious during growth on methanol (when this cytochrome has a specific function) than on methylamine. The concentrations of blue copper proteins were highest at the copper concentrations which supported maximum growth (except for the absence of amicyanin during growth on methanol). In the absence of added copper, amicyanin could not be detected, and in the absence of added iron neither amicyanin nor ‘azurin’ was detectable. The most important conclusions are that high concentrations of amicyanin may not be essential for methylamine oxidation, that ‘azurin’ may replace cytochrome c for some electron-transport functions, and that iron is required for synthesis of blue copper proteins.
Beardmore-GrayM., O’KeeffeD.T., AnthonyC.1983; The methanol: cytochrome coxidoreduc- tase activity of methylotrophs.. Journal of General Microbiology 129:923–933
De BeerR., DuineJ.A., FrankJ., LargeP.J.1980; The prosthetic group of methylamine dehydrogenase from Pseudomonas AM1.. Biochimica et biophysicaacta 622:370–374
EadyR.R., LargeP.J.1968; Purification and properties of an amine dehydrogenase from Pseudomonas AMI and its role in growth on methylamine.. Biochemical Journal 106:245–255
EadyR.R., LargeP.J.1971; Microbial oxidation of amines.Spectral and kinetic properties of the primary amine dehydrogenase of Pseudomonas AM1.. Biochemical Journal 123:757–771
FukumoriY., YamanakaT.1987; The methylamine oxidising system of Pseudomonas AM1 reconstituted from purified components.. Journal of Biochemistry 101:441–445
JohanidesV., VrdoljakM., MaricV.1979; A selection of methylotrophic bacteria for single cell protein production from methanol.. Acta biologica jugoslavica - mikrobiolojica 16:1–9
KatesM.1972; Techniques of lipidology.. In Laboratory Techniques in Biochemistry and Molecular Biology3WorkT. S., WorkD. Edited by Amsterdam: North Holland Publishing Company;
LawtonS.A., AnthonyC.1985a; The role of blue copper proteins in the oxidation of methylamine by an obligate methylotroph.. Biochemical Journal 228:719–725
LawtonS.A., AnthonyC.1985b; The roles of cytochromes and blue copper proteins in the oxidation of methanol and methylamine in organism 4025, an obligate methylotroph.. Journal of General Microbiology 131:2165–2171
SmithA., HillS., AnthonyC.1988; A haemoprotein is not involved in the control by oxygen of enteric nitrogenase synthesis.. Journal of General Microbiology 134:1499–1507
TobariJ.1984; Blue copper proteins in electron transport in methylotrophic bacteria.. In Microbial Growth on C1-compounds pp. 106–112CrawfordC. L., HansonR. S. Edited by Washington, DC: American Society for Microbiology;
VrdoljakM., FroudS.J.1982; Characterisation of the electron transport chain of an obligate methylotroph strain 4025.. International Journal of Biochemistry 14:1019–1023
VrdoljakM., MaricV., JohanidesV.1984; Copper requirement and its influence on the growth of the obligate methylotrophic bacterial strain 4025.. Biotechnology Letters 6:501–506