4a It is also commonly used as a more general

phenomenol

4a. It is also commonly used as a more general

phenomenological equation to fit data and has been directly applied to quantify the relationship between lumen pH and qE, as in Fig. 4b. The Hill equation has the form $$ F = \frac[H^+]^n [H^+]^n +[10^-p\it K_a]^n, $$ (3)where F is the fraction of proteins that are activated. The Hill equation contains two parameters: the pK a, which is the pH at which F = 0.5, and the Hill coefficient n, which is Selleckchem Lazertinib a measure of the sigmoidicity, or “steepness,” of the transition of F from a “100 % on” state to a “100 % off” state. In the case when a protein must bind multiple protons to be activated, and when this binding is highly cooperative, the Hill coefficient n can be interpreted as the number of protons needed to activate the protein, as in the reaction $$ A + n H^+ \rightleftharpoons A H^+_n. $$ (4) In the case when binding is not extremely cooperative, the Hill coefficient still measures the cooperativity of binding, but does not correspond directly

to a physical property such as the number of protonatable sites (Weiss 1997). The existing measurements from several labs fit quite well to the Hill equation. However, the Hill equation does not directly correspond to a physical model in most situations (Weiss 1997). As a Rigosertib result, extracting mechanistic Selinexor manufacturer information from measurements of qE measured as a function of lumen pH is challenging. One way forward is through the development of physically motivated mathematical models that explicitly incorporate each protonation event in various hypotheses of qE mechanism. In the following sections, we review measurements correlating lumen pH and the hypotheses that have been generated from these measurements. Measurements of qE triggering ΔpH or low lumen pH? For understanding the processes triggering qE, it is important to differentiate between those processes that only require a low lumen pH and processes that require a \(\Updelta\hboxpH\) across the thylakoid membrane. The protonation of residues in PsbS, VDE, and LHC proteins can be accomplished by lowering

the lumen pH, without necessarily requiring a pH gradient Histone demethylase across the thylakoid membrane. However, work by Goss et al. (2008) demonstrated that a pH gradient across the thylakoid membrane, along with a neutral or slightly basic stromal pH, is required for the formation of zeaxanthin-dependent qE. Once qE is formed, it is possible to maintain qE even in the absence of a pH gradient if the lumen pH is kept sufficiently low (Rees et al. 1992). This property was used to determine the qE versus pH curves in Johnson and Ruban (2011) and Johnson et al. (2012). The ability to maintain qE in low pH, even without a \(\Updelta\hboxpH,\) suggests that the \(\Updelta\hboxpH\) is required for proper insertion of zeaxanthin (Goss et al. 2008), but that other pH-sensitive components of qE do not require a pH gradient.

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