How the Electron-Transfer Cascade is Maintained in Chlorophyll-d Containing Photosystem I.

Abstract

Photosystem I (PSI) from Acaryochloris marina utilizes chlorophyll d (Chld) with a formyl group as its primary pigment, which is more red-shifted than chlorophyll a (Chla) in PSI from Thermosynechococcus elongatus. Using the cryo-electron microscopy structure and solving the linear Poisson-Boltzmann equation, here we report the redox potential (Em) values in A. marina PSI. The Em(Chld) values at the paired chlorophyll site, [PAPB], are nearly identical to the corresponding Em(Chla) values in T. elongatus PSI, despite Chld having a 200 mV lower reduction power. The accessory chlorophyll site, A-1, in the B branch exhibits an extensive H-bond network with its ligand water molecule, contributing to Em(A-1B) being lower than Em(A-1A). The substitution of pheophytin a (Pheoa) with Chla at the electron acceptor site, A0, decreases Em(A0), resulting in an uphill electron transfer from A-1. The impact of the A-1 formyl group on Em(A0) is offset by the reorientation of the A0 ester group. It seems likely that Pheoa is necessary for A. marina PSI to maintain the overall electron-transfer cascade characteristic of PSI in its unique light environment.