Advances in Microbial Physiology - download pdf or read online

By R.K. Poole (Eds.)

ISBN-10: 0120277409

ISBN-13: 9780120277407

This quantity is a part of a chain which gives debts of growth in microbial biology.

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Many methylotrophs are therefore unusual in having growth that is limited by reductant (NADH) rather than by ATP availability, a conclusion of considerable importance when predicting growth yields on methanol and methane (Anthony, 1986). , 1972a; Anthony, 1982). I . 2. lpe I and Type 11 Periplasmic Alcohol Dehj)drogenases The role of the type I quinoprotein alcohol dehydrogenase in P . aeruginosa and P . , 1995). Although the affinity of this enzyme for methanol is low, in Rhodopseudomonas acidophila it can also function in energy production during anaerobic growth on methanol in the light; in this case it has a role in the production of reducing power by reverse electron transfer (Anthony, 1982).

During growth on ethanol. A similar electron transport chain presumably operates in P . , 1995). The electron acceptor for the type I1 alcohol dehydrogenases (quinohaemoproteins) in C. testosteroni and P . putidu is not known but, because 40 PAT M. GOODWIN AND CHRIS ANTHONY this is a periplasmic enzyme, it is likely to be a specific cytochrome c or blue copper protein (Fig. 14). 2. Electron Transport Chains involving Membrane-bound Quinohaemoprotein Alcohol Dehydrogenase (Type 111) in Acetic Acid Bacteria This type of enzyme has only been described in acetic acid bacteria, which are strict aerobes and have highly active oxidase systems for metabolizing sugars and alcohols.

Bo cyt. of ADH Figure 15 - 02 0, - 0, - [ High oxygen tension ] [Low oxygen tension] cyanidesensitive - alternative oxldase cyanide insensitive o2 Electron transport chains involved in the oxidation of glucose. 42 PAT M. GOODWIN AND CHRIS ANTHONY In P . , 1982b). , 1997). As is often the case. the situation with the acetic acid bacteria is complex. , 1987). At low pH, however, a second ‘cyanide-insensitive’ and non-energygenerating pathway appears to operate. , 1989c, 1994). Many of the systems for glucose oxidation shown in Fig.

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Advances in Microbial Physiology by R.K. Poole (Eds.)

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