Thermodynamic Factors Controlling Electron Transfer among the Terminal Electron Acceptors of Photosystem I: Insights from Kinetic Modelling.
(phyllo)quinone
electron transfer
iron–sulphur cluster
reorganisation energy
standard Gibbs free energy difference
tunnelling barrier
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
10 Sep 2024
10 Sep 2024
Historique:
received:
07
08
2024
revised:
30
08
2024
accepted:
05
09
2024
medline:
28
9
2024
pubmed:
28
9
2024
entrez:
28
9
2024
Statut:
epublish
Résumé
Photosystem I is a key component of primary energy conversion in oxygenic photosynthesis. Electron transfer reactions in Photosystem I take place across two parallel electron transfer chains that converge after a few electron transfer steps, sharing both the terminal electron acceptors, which are a series of three iron-sulphur (Fe-S) clusters known as FX, FA, and FB, and the terminal donor, P700. The two electron transfer chains show kinetic differences which are, due to their close geometrical symmetry, mainly attributable to the tuning of the physicochemical reactivity of the bound cofactors, exerted by the protein surroundings. The factors controlling the rate of electron transfer between the terminal Fe-S clusters are still not fully understood due to the difficulties of monitoring these events directly. Here we present a discussion concerning the driving forces associated with electron transfer between FX and FA as well as between FA and FB, employing a tunnelling-based description of the reaction rates coupled with the kinetic modelling of forward and recombination reactions. It is concluded that the reorganisation energy for FX- oxidation shall be lower than 1 eV. Moreover, it is suggested that the analysis of mutants with altered FA redox properties can also provide useful information concerning the upstream phylloquinone cofactor energetics.
Identifiants
pubmed: 39337283
pii: ijms25189795
doi: 10.3390/ijms25189795
pii:
doi:
Substances chimiques
Photosystem I Protein Complex
0
Iron-Sulfur Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Regione Lombardia
ID : DSS 16652 30/11/2021
Organisme : Italian Ministry of University and Research (MUR)
ID : 20224HJWMH