bo oxidase 2: bd oxidase 1: NDH-I ≥1.5 unitless
||Bacteria Escherichia coli
||Sauer U, Bailey JE. Estimation of P-to-O ratio in Bacillus subtilis and its influence on maximum riboflavin yield. Biotechnol Bioeng. 1999 Sep 20 64(6):750-4. DOI: 10.1002/(SICI)1097-0290(19990920)64:6<750::AID-BIT15>3.0.CO2-S link p.752 left column bottom paragraph PubMed ID10417225
||Unden G, Bongaerts J. 1997. Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochim Biophys Acta 1320: 217–234. AND Bogachev AV, Murtazina RA, Skulachev VP. 1996. H+/e− stoichiometry for NADH dehydrogenase I and dimethyl sulfoxide reductase in anaerobically grown Escherichia coli cells. J Bacteriol 178: 6233–6237.PubMed ID9230919, 8892824
||Abstract: "Simultaneous growth and riboflavin overproduction were investigated using a previously developed stoichiometric model of Bacillus subtilis metabolism. A fit of model predictions to experimental data was used to obtain estimates of fundamental energetic parameters of B. subtilis." P.750 right column bottom paragraph: "A previously constructed stoichiometric model of B. subtilis
metabolism was used as published (Sauer et al., 1998). Briefly, mass balances on cellular metabolites provide a set of linear equations relating intracellular and external fluxes."
||P.752 left column bottom paragraph: "Multiple terminal oxidases, which catalyze the transfer of electrons to oxygen with different energy-coupling efficiencies, exist in bacteria with branched electron transport chains such as E. coli and B. subtilis. In E. coli, the H+/e−
stoichiometry of the terminal bo and bd oxidases was determined to be 2 and 1, respectively (primary source Unden and Bongaerts, 1997), and at least 1.5 for NDH-I (primary source Bogachev, et al., 1996)."