Secretion of both partially unfolded and folded apoproteins of dimethyl sulfoxide reductase by spheroplasts from a molybdenum cofactor-deficient mutant of Rhodobacter sphaeroides f. sp. dentrificans

A study investigated the secretion of both partially unfolded and folded apoproteins of dimethyl sulfoxide (DMSO) reductase by spheroplasts from a molybdenum cofactor-deficient mutant of Rhodobacter sphaeroides f. sp. dentrificans. Results suggest that form II was a partially unfolded but compactly...

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Bibliographic Details
Published inJournal of bacteriology Vol. 176; no. 6; p. 1624
Main Authors Masui, Hideo, Satoh, Michihiro, Satoh, Toshio
Format Journal Article
LanguageEnglish
Published Washington American Society for Microbiology 01.03.1994
Subjects
Bacteriology
Enzymes
Mutation
Proteins
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Summary:A study investigated the secretion of both partially unfolded and folded apoproteins of dimethyl sulfoxide (DMSO) reductase by spheroplasts from a molybdenum cofactor-deficient mutant of Rhodobacter sphaeroides f. sp. dentrificans. Results suggest that form II was a partially unfolded but compactly folded apoprotein of DMSO reductase.
ISSN:0021-9193
1098-5530