By R.K. Poole (Eds.)
This quantity is a part of a sequence which gives debts of development in microbial biology.
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Pyruvateeformate lyase) are oxygen-sensitive, but are induced before conditions become completely anaerobic; they must, therefore, be protected from the remaining oxygen. To achieve this it is essential to have a source of electrons for rapid electron transfer to consume oxygen by way of the high-affinity oxidase (cytochrome hd) which is also induced during these conditions. Glucose dehydrogenase, which supports a high rate of respiration, could provide this. There is some evidence for such a role for glucose dehydrogenase in protecting the oxygensensitive pyruvate metabolism and nitrogenase in conditions supporting microaerobic nitrogen fixation in K .
1992b). Usually reconstitution of membrane enzymes into proteoliposomes requires incubation of all the components together. However, in the case of the type 111 quinohaemoprotein alcohol dehydrogenase it was possible to reconstitute an active system by addition of the enzyme to preformed proteoliposomes containing the oxidases. 2). There is some evidence that subunit 11 (the tri-haem cytochrome c) may also be able to mediate electron transfer from membrane glucose dehydrogenase (see below) but the physiological significance of this has yet to be determined.
Methanol dehydrogenase Methylotrophic bacteria are able to grow on reduced carbon compounds such as methane or methanol. Methane is produced in anaerobic environments by methanogenic bacteria and this provides a substrate for growth of methanotrophs at the aerobic surface. As well as being a product of methane oxidation, methanol arises in nature by hydrolysis of methyl ethers and esters present in pectin and lignin which are structural components of plants; methylotrophs growing on methanol are therefore abundant on the surfaces of leaves and in soil and water (Anthony, 1982).