ISOLATION AND CHARACTERIZATION OF A STRAIN OF RHODOBACTER-SULFIDOPHILUS - A BACTERIUM WHICH GROWS AUTOTROPHICALLY WITH DIMETHYLSULFIDE AS ELECTRON-DONOR

被引:45
作者
HANLON, SP
HOLT, RA
MOORE, GR
MCEWAN, AG
机构
[1] UNIV E ANGLIA,SCH BIOL SCI,CTR METALLOPROT SPECT & BIOL,NORWICH NR4 7TJ,NORFOLK,ENGLAND
[2] UNIV E ANGLIA,SCH CHEM SCI,NORWICH NR4 7TJ,NORFOLK,ENGLAND
[3] ZENECA BIO PROD,BILLINGHAM TS23 1YN,CLEVELAND,ENGLAND
来源
MICROBIOLOGY-UK | 1994年 / 140卷
关键词
DIMETHYLSULFIDE OXIDATION; RHODOBACTER SULFIDOPHILUS;
D O I
10.1099/13500872-140-8-1953
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
A marine photosynthetic bacterium (strain SH1) was isolated after enrichment under phototrophic conditions in media containing dimethylsulphide (DMS) and bicarbonate (HCO3-) as potential carbon sources. Analysis of culture medium using nuclear magnetic resonance spectrometry showed that during phototrophic and chemotrophic growth of strain SH1 on DMS/HCO3- dimethylsulphoxide (DMSO) was produced from DMS. These results indicate that strain SH1 grew autotrophically with DMS serving as an electron donor in photosynthesis and respiration, but not as a carbon source. Biochemical characterization and 165 rRNA analysis indicated that the isolate was a strain of Rhodobacter sulfidophilus. An assay for the enzyme catalysing the oxidation of DMS (DMS:acceptor oxidoreductase) was developed by measuring electron transfer from DMS to 2,6-dichlorophenolindophenol (DCPIP). This reaction was dependent on phenazine ethosulphate to mediate electron transfer from DMS:acceptor oxidoreductase to DCPIP. DMS:acceptor oxidoreductase was found to have a periplasmic location in strain SH1 as was a reduced methylviologen:DMSO oxidoreductase activity. Zymogram staining patterns of periplasmic fractions indicated that DMS: acceptor oxidoreductase and DMSO reductase were distinct enzymes. This was confirmed by resolution of the two activities by gel filtration.
引用
收藏
页码:1953 / 1958
页数:6
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