Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
INVESTIGATION OF THE FUMARATE METABOLISM OF THE SYNTROPHIC PROPIONATE-OXIDIZING BACTERIUM STRAIN MPOB
Autore:
VANKUIJK BLM; SCHLOSSER E; STAMS AJM;
Indirizzi:
AGR UNIV WAGENINGEN,MICROBIOL LAB,HESSELINK SUCHTELENWEG 4 NL-6703 CTWAGENINGEN NETHERLANDS AGR UNIV WAGENINGEN,MICROBIOL LAB NL-6703 CT WAGENINGEN NETHERLANDS
Titolo Testata:
Archives of microbiology
fascicolo: 4, volume: 169, anno: 1998,
pagine: 346 - 352
SICI:
0302-8933(1998)169:4<346:IOTFMO>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
REVERSED ELECTRON-TRANSPORT; VIBRIO-SUCCINOGENES; ESCHERICHIA-COLI; ANAEROBIC-BACTERIA; MEMBRANE-VESICLES; ACETATE OXIDATION; L-MALATE; FORMATE; PATHWAY; GROWTH;
Keywords:
SYNTROPHY; FUMARATE REDUCTION; PROPIONATE OXIDATION; ANAEROBIC GROWTH; ELECTRON TRANSPORT CHAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
B.L.M. Vankuijk et al., "INVESTIGATION OF THE FUMARATE METABOLISM OF THE SYNTROPHIC PROPIONATE-OXIDIZING BACTERIUM STRAIN MPOB", Archives of microbiology, 169(4), 1998, pp. 346-352

Abstract

The growth of the syntrophic propionate-oxidizing bacterium strain MPOB in pure culture by fumarate disproportionation into carbon dioxide and succinate and by fumarate reduction with propionate, formate or hydrogen as electron donor was studied. The highest growth yield, 12.2 gdry cells/mol fumarate, was observed for growth by fumarate disproportionation. In the presence of hydrogen, formate or propionate, the growth yield was more than twice as low: 4.8, 4.6, and 5.2 g dry cells/mol fumarate, respectively. The location of enzymes that are involved inthe electron transport chain during fumarate reduction in strain MPOBwas analyzed. Fumarate reductase, succinate dehydrogenase, and ATPasewere membrane-bound, while formate dehydrogenase and hydrogenase wereloosely attached to the periplasmic side of the membrane. The cells contained cytochrome c, cytochrome b, menaquinone-6 and menaquinone-7 as possible electron carriers. Fumarate reduction with hydrogen in membranes of strain MPOB was inhibited by 2-(heptyl)4-hydroxyquinoline-N-oxide (HOQNO). This inhibition, together with the activity of fumarate reductase with reduced 2,3-dimethyl-1,4-naphtoquinone (DMNH2) and the observation that cytochrome b of strain MPOB was oxidized by fumarate,suggested that menequinone and cytochrome b are involved in the electron transport during fumarate reduction in strain MPOB. The growth yields of fumarate reduction with hydrogen or formate as electron donor were similar to the growth yield of Wolinella succinogenes. Therefore, it can be assumed that strain MPOB gains the same amount of ATP from fumarate reduction as W. succinogenes, i.e. 0.7 mel ATP/mol fumarate. This value supports the hypothesis that syntrophic propionate-oxidizingbacteria have to invest two-thirds of an ATP via reversed electron transport in the succinate oxidation step during the oxidation of propionate. The same electron transport chain that is involved in fumarate reduction may operate in the reversed direction to drive the energetically unfavourable oxidation of succinate during syntrophic propionate oxidation since (1) cytochrome b was reduced by succinate and (2) succinate oxidation was similarly inhibited by HOQNO as fumarate reduction.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/20 alle ore 06:24:43