TRIMETHYLAMINE OXIDE RESPIRATION IN PROTEUS SP STRAIN NTHC153 - ELECTRON TRANSFER-DEPENDENT PHOSPHORYLATION AND L-SERINE TRANSPORT
TRIMETHYLAMINE OXIDE RESPIRATION IN PROTEUS SP STRAIN NTHC153 - ELECTRON TRANSFER-DEPENDENT PHOSPHORYLATION AND L-SERINE TRANSPORT
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DOI:
10.1128/jb.149.1.22-28.1982
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发表时间:
1982-01-01
影响因子:
3.2
通讯作者:
STROM, AR
中科院分区:
文献类型:
--
作者:
STENBERG, E;STYRVOLD, OB;STROM, AR
Cells of Proteus sp. strain NTHC153 grown anaerobically with glucose and trimethylamine oxide (TMAO) were converted to spheroplasts by the penicillin method. The spheroplasts were lysed by osmotic shock, and the membrane vesicles were purified by sucrose gradient centrifugation. Vesicles energized by electron transfer from formate to TMAO displayed active anaerobic transport of serine. An anaerobic cell-free extract of Proteus sp. disrupted in a French pressure cell reduced TMAO with formate and NADH with the concomitant formation of organic phosphate. The net P/2e- ratios determined were 0.1 and 0.3, respectively. The NADH- and TMAO-dependent phosphorylation was sensitive to uncouplers of oxidative phosphorylation (protonophores), and formate- and TMAO-dependent serine transport activities were sensitive to ionophores and protonophores. TMAO reduction in Proteus sp. evidently fulfills the essential features of anaerobic respiration.