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New PDF release: Advances in Microbial Physiology

By R.K. Poole (Eds.)

ISBN-10: 0120277409

ISBN-13: 9780120277407

This quantity is a part of a sequence which gives bills of growth in microbial biology.

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Extra resources for Advances in Microbial Physiology

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Free aldehydes have not been detected during the oxidation of ethanol to acetic acid and these two enzymes are responsible for the production of acetic acid from ethanol which is characteristic of acetic acid bacteria. The aldehyde dehydrogenase has two or three subunits, one being a cytochrome c component and the other originally thought to contain PQQ. , 1994). , 1989). The 20 PAT M. GOODWIN AND CHRIS ANTHONY electron acceptor for these membrane aldehyde dehydrogenases has not been identified, but as there is usually no cytochrome c oxidase in these bacteria it is probable that electrons are passed to the cytochrome subunit and thence to ubiquinone in the membrane, as shown in the alcohol dehydrogenases of these bacteria.

For example, using the same mutant of A . 3 nM) (Matsushita e f al.. 1995a). The metal content of the reconstituted holoen- 26 PAT M. GOODWIN AND CHRIS ANTHONY zyme cannot be determined because the process is readily reversible, and removal of the excess Mg2+ required for reconstitution will also remove the ion from the enzyme. If the function of the metal ion during reconstitution is to provide a metal ion at the active site, then this will have implications for our understanding of the mechanism of glucose dehydrogenase, as it is unlikely that Mg2+ could replace Ca2+ for some functions.

Presumably assembly of the holoenzyme in the periplasm is facilitated by MxaA, and possibly also by the membrane protein MxaL. Geiger and Gorisch (1989) had previously shown that, in solution, PQQ forms a complex with Ca2+ or Mg2+; the complex has an absorption maximum of 343 nm, different from that of free PQQ (330 nm) but very similar to that of PQQ in alcohol dehydrogenases. They concluded that either the ion is necessary to induce the proper conformation of the protein so that i t can then bind PQQ at the active site, or that PQQ is anchored as a complex with the calcium.

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

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