Characterisation of a red form of methanol dehydrogenase from the marine methylotrophMethylophaga marina
In: FEMS Microbiology Letters, Jg. 97 (1992-10-01), S. 293-297
Online
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Zugriff:
The quinoprotein methanol dehydrogenase (MDH) of the marine methylotroph Methylophaga marina is similar to that of other methylotrophs in being an α2β2 tetramer containing two molecules of PQQ and a single atom of calcium. Its electron acceptor is cytochrome cL and interaction of the two proteins is by way of carboxylates on the cytochrome and lysyl residues on the α subunit of MDH. The reaction was not, however, sensitive to high ionic strength as was the reaction in non-halophilic bacteria. A red form of the enzyme was sometimes produced which had a low specific activity and a low calcium content. Activity was restored by incubation with Ca2+ which also produced the typical (green) enzyme, with a typical absorption spectrum. This provides the first demonstration of reconstitution of active MDH from enzyme lacking calcium isolated from a wild-type methylotroph.
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Characterisation of a red form of methanol dehydrogenase from the marine methylotrophMethylophaga marina
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Autor/in / Beteiligte Person: | Anthony, Christopher ; Chan, H.T.C. |
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Zeitschrift: | FEMS Microbiology Letters, Jg. 97 (1992-10-01), S. 293-297 |
Veröffentlichung: | Oxford University Press (OUP), 1992 |
Medientyp: | unknown |
ISSN: | 1574-6968 (print) ; 0378-1097 (print) |
DOI: | 10.1111/j.1574-6968.1992.tb05478.x |
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