Difference between revisions of "PM-pathway control state"
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[[File:PM.jpg|right|400px|link=Gnaiger 2014 MitoPathways |Gnaiger 2014 MitoPathways - Chapter 3.2]] | [[File:PM.jpg|right|400px|link=Gnaiger 2014 MitoPathways |Gnaiger 2014 MitoPathways - Chapter 3.2]] | ||
== PM(L) == | == PM(L) == | ||
Revision as of 15:33, 25 January 2016
- high-resolution terminology - matching measurements at high-resolution
PM-pathway control state
Description
MitoPathway control: CI
SUIT protocol: SUIT-RP1
Pyruvate (P) is oxidatively decarboxylated to acetyl-CoA and CO2, yielding NADH catalyzed by pyruvate dehydrogenase. Malate (M) is oxidized to oxaloacetate by mt-malate dehydrogenase located in the mitochondrial matrix. Condensation of oxaloacate with acetyl-CoA yields citrate (citrate synthase). 2-oxoglutarate (Ξ±-ketoglutarate) is formed from isocitrate (isocitrate dehydrogenase).
Abbreviation: PM
Reference: Gnaiger 2014 MitoPathways - Chapter 3.2
PM(L)
- SUIT-RP1: 1PM 2D 2c (2NADH) 3U 4Oct 5G 6S 7Rot 8Gp 9Ama 10Tm
PM(P)
- SUIT-RP1: 1PM 2D 2c (2NADH) 3U 4Oct 5G 6S 7Rot 8Gp 9Ama 10Tm
PM(E)
- SUIT-RP1: 1PM 2D 2c (2NADH) 3U 4Oct 5G 6S 7Rot 8Gp 9Ama 10Tm
CI-linked linear coupling control: L β P - E
- L - P
- OXPHOS coupling efficiency (P-L or βP control factor), jβP = βP/P = (P-L)/P = 1-L/P, is measured in the CI-linked substrate state, with defined coupling sites (CI, CIII, CIV) and at high flux.
- P - E
- CCCP is titrated stepwise to maximum flux, to evaluate limitation of OXPHOS by the phosphorylation system, expressed as the apparent excess E-P capacity factor (E-P coupling control factor), jExP = (E-P)/E = 1-P/E. If jExP>0, then the ETS coupling efficiency rather than the OXPHOS coupling efficiency is the proper expression of coupling, jβE = βE/E = (E-L)/E = 1-L/E.
Discussion
- Pyruvate alone is not an ETS competent substrate state in most mt-preparations, since acetyl-CoA accumulates without the co-substrate (oxaloacetate) of citrate synthase.
- Malate alone is not an ETS competent substrate state in many mt-preparations, since oxaloacetate accumulates without the co-substrate (acetyl-CoA) of citrate synthase.
