1887

Abstract

Summary: Organism 4025 contained only -type and -type cytochromes. In the absence of any -type cytochrome oxidase it was concluded that respiration in these bacteria is catalysed entirely by way of the -type cytochrome oxidase. After growth on methanol, the soluble protein contained cytochromes and , and a single blue copper protein of unknown function, ‘azurin'. After growth on methylamine the soluble proteins were strikingly different. The total concentration of soluble cytochrome was about 70% lower; cytochrome c was about 65%, and cytochrome c about 16% of the concentrations present after growth on methanol. Although some ‘azurin’ was still present, a second copper protein, amicyanin (94% of the total), was induced during growth on methylamine. The concentration of this protein was considerably higher than that of blue copper proteins measured in other bacteria and 35 times higher than the concentration in the facultative methylotroph AMI during growth on methylamine. It is the very high concentration of amicyanin that gave suspensions of methylamine-grown organism 4025 their blue-green colour. All of the soluble cytochrome , and all of the methanol dehydrogenase, methylamine dehydrogenase and blue copper proteins were located in the periplasmic fraction. All these results are consistent with the conclusion that the main electron acceptor for methylamine dehydrogenase in organism 4025 is amicyanin.

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/content/journal/micro/10.1099/00221287-131-9-2165
1985-09-01
2019-10-24
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-131-9-2165
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