1887

Abstract

Three classes of Hup mutants of were obtained by -methyl-′-nitro--nitrosoguanidine mutagenesis and screening by HH uptake: (1) those with no discernible H-uptake or H-evolving activity, (2) those showing no uptake but some H production and (3) those leaky for both activities. One mutant strain, MCD-124, expressed hydrogenase activity similar to the solubilized wild-type enzyme in O sensitivity, sedimenting behaviour and pH optimum. All the other mutants were probably mutated in the hydrogenase structural or processing (methylene blue) genes rather than in genes for hydrogenase-linked respiratory proteins. Four mutants chosen from the first category were complemented for hydrogenase activity by conjugation with carrying plasmid pHU1 containing hydrogenase genes. A pHU1 transconjugant of strain MCD-124, on the other hand, did not express any additional hydrogenase activity.

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/content/journal/micro/10.1099/00221287-131-6-1459
1985-06-01
2019-10-20
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