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

By R.K. Poole (Eds.)

This quantity is a part of a sequence which supplies bills of development in microbial biology.

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Although these observations demonstrated a requirement for divalent metal ions for insertion of PQQ into the enzymes, they provided no indication of whether or not the metal ions had been incorporated as structural or functional components of the active enzymes. 1. Calcium in Methanol Dehydrogenase and Other Alcohol Dehydrogenases The only enzyme for which a structure is available is methanol dehydrogenase, which has a Ca2+ ion tightly coordinated to the PQQ in the active site (Fig. 4; Section 5).

Dotted lines indicate alternative routes of electron transfer. 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.

1995; Anthony, 1996). 2. The Structures and Mechanisms of Alcohol and Glucose Dehydrogenases The model alcohol dehydrogenase being considered here is the N-terminal region of subunit I of the type 111 alcohol dehydrogenase of acetic acid PQQ AND QUINOPROTEINS 31 Figure 9 The novel disulphide ring in the active site of methanol dehydrogenase. The ring is formed by disulphide bond formation between adjacent cysteine residues. The PQQ is 'sandwiched' between this ring and the tryptophan that forms the floor of the active site chamber.

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