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. 2006 Jan 31;2:2006.0004. doi: 10.1038/msb4100046

Figure 4.

Figure 4

The effect of the Ech hydrogenase reaction stoichiometry on growth yields. (A) Variability in the growth-associated maintenance (GAM) that will produce growth yields consistent with experimental data. This variability is shown as a function of Ech hydrogenase reaction stoichiometry. Yields were calculated using iAF692 for four different substrates (methanol, acetate, H2/CO2 and pyruvate). Panel A shows the total GAM variability across all substrates. (B, C) GAM variability for each substrate at a constant Ech hydrogenase reaction stoichiometry (0.2 protons translocated/2e− (B, green) and 1.1 protons translocated/2e− (C, purple)). The ranges calculated were constrained by experimental values. (D) A diagram of all energy-conserving ion translocating reactions in M. barkeri, each labeled with the stoichiometry of the translocated ion. Any value greater than 2 protons translocated/2e− for Ech hydrogenase created a larger total GAM range across all substrates. ATPS, ATP synthase; MTSPCMMT, methyl-H4SPT:coenzyme M methyltransferase; HDR, heterodisulfide reductase; F4NRH, F420-nonreducing hydrogenase; F4D, F420H2 dehydrogenase; ECHH, Ech hydrogenase; MCR, methyl-coenzyme M reductase; F4RH, F420-reducing hydrogenase; Pi, pyrophosphate; com, coenzyme m, mh4spt, methyl-tetrahydrosarcinapterin, h4spt, tetrahydrosarcinapterin; mcom, methyl-coenzyme M; cob, coenzyme B; hsfd, heterodisulfide; mphen, oxidized methanophenazine; mphenH2, reduced methanophenazine; F420H2, reduced coenzyme F420; F420, oxidized coenzyme F420; fd-red, reduced ferredoxin; fd-ox, oxidized ferredoxin.