title: How does the QB site influence propagate to the QA site in photosystem II?
abstract: The redox potential of the primary quinone Q(A) [E(m)(Q(A))] in photosystem II (PSII) is lowered by replacement of the native plastoquinone (PQ) with bromoxynil (BR) at the secondary quinone Q(B) binding site. Using the BR-bound PSII structure presented in the previous Fourier transform infrared and docking calculation studies, we calculated E(m)(Q(A)) considering both the protein environment in atomic detail and the protonation pattern of the titratable residues. The calculated E(m)(Q(A)) shift in response to the replacement of PQ with deprotonated BR at the Q(B) binding site [ΔE(m)(Q(A))(PQ→BR)] was -55 mV when the three regions, Q(A), the non-heme iron complex, and Q(B) (Q(B) = PQ or BR), were treated as a conjugated supramolecule (Q(A)-Fe-Q(B)). The negative charge of BR apparently contributes to the downshift in ΔE(m)(Q(A))(PQ→BR). This downshift, however, is mostly offset by the influence of the residues near Q(B). The charge delocalization over the Q(A)-Fe-Q(B) complex and the resulting H-bond strength change between Q(A) and D2-His214 are crucial factors that yield a ΔE(m)(Q(A))(PQ→BR) of -55 mV by (i) altering the electrostatic influence of the H-bond donor D2-His214 on E(m)(Q(A)) and (ii) suppressing the proton uptake events of the titratable residues that could otherwise upshift ΔE(m)(Q(A))(PQ→BR) during replacement of PQ with BR at the Q(B) site.
authors.affiliation: Career-Path Promotion Unit for Young Life Scientists, Graduate School of Medicine, Kyoto University, Yoshida-Konoe-cho, Sakyo-ku, Kyoto 606-8501, Japan. hiro@cp.kyoto-u.ac.jp
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Ishikita
authors.forename: Koji
authors.initials: K
authors.lastname: Hasegawa
authors.forename: Takumi
authors.initials: T
authors.lastname: Noguchi
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry; D001665:Binding Sites; D000458:Cyanobacteria / Q000737:chemistry; D008958:Models, Molecular; D015394:Molecular Structure; D009570:Nitriles / Q000737:chemistry; D045332:Photosystem II Protein Complex / Q000737:chemistry*; D010971:Plastoquinone / Q000737:chemistry; D011522:Protons; D011809:Quinones / Q000737:chemistry; D055672:Static Electricity
chemical_list: D001426:Bacterial Proteins; D009570:Nitriles; D045332:Photosystem II Protein Complex; D011522:Protons; D011809:Quinones; C006826:bromoxynil; D010971:Plastoquinone