Flavodoxin from Wolinella succinogenes

被引:9
作者
Biel, S [1 ]
Klimmek, O [1 ]
Gross, R [1 ]
Kroger, A [1 ]
机构
[1] UNIV FRANKFURT,INST MIKROBIOL,D-60439 FRANKFURT,GERMANY
关键词
flavodoxin; Wolinella succinogenes; pyruvate synthase;
D O I
10.1007/s002030050365
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
A momomeric flavoprotein (18.8 kDa) was isolated from the soluble cell fraction of Wolinella succinogenes and was identified as a flavodoxin based on its N-terminal sequence, FMN content, and redox properties. The midpoint potentials of the flavodoxin (Fld) at pH 7.5 were measured as -95 mV (Fld(ox)/Fld(s)) and -450 mV (Fld(s)/Fld(red)) relative to the standard hydrogen electrode. The cellular flavodoxin content [0.3 mu mol (g protein)(-1)] was same in bacteria grown with fumarate or with polysulfide as the terminal acceptor of electron transport. The flavodoxin did not accept electrons from hydrogenase or formate dehydrogenase, the donor enzymes of electron transport to fumarate or polysulfide. Pyruvate:flavodoxin oxidoreductase activity [180 U (g cellular protein)(-1)] was detected in the soluble cell fraction of W. succinogenes grown with fumarate or polysulfide. The enzyme was equally active with Fld(ox) or Fld(s) at high concentrations. The K-m for Fld(s) (80 mu M) was larger than that for Fld(ox) and for the ferredoxin isolated from W. succinogenes (15 mu M). We conclude that flavodoxin serves anabolic rather than catabolic functions in W. succinogenes.
引用
收藏
页码:122 / 127
页数:6
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