Redox potential of the non-heme iron complex in bacterial photosynthetic reaction center.
In bacterial photosynthetic reaction centers (bRC), the electron is transferred from the special pair (P) via accessory bacteriochlorophyll (B(A)), bacteriopheopytin (H(A)), the primary quinone (Q(A)) to the secondary quinone (Q(B)). Although the non-heme iron complex (Fe complex) is located between Q(A) and Q(B), it was generally supposed not to be redox-active. Involvement of the Fe complex in electron transfer (ET) was proposed in recent FTIR studies [A. Remy and K. Gerwert, Coupling of light-induced electron transfer to proton uptake in photosynthesis, Nat. Struct. Biol. 10 (2003) 637-644]. However, other FTIR studies resulted in opposite results [J. Breton, Steady-state FTIR spectra of the photoreduction of Q(A) and Q(B) in Rhodobacter sphaeroides reaction centers provide evidence against the presence of a proposed transient electron acceptor X between the two quinones, Biochemistry 46 (2007) 4459-4465]. In this study, we calculated redox potentials of Q(A/B) (E(m)(Q(A/B))) and the Fe complex (E(m)(Fe)) based on crystal structure of the wild-type bRC (WT-bRC), and we investigated the energetics of the system where the Fe complex is assumed to be involved in the ET. E(m)(Fe) in WT-bRC is much less pH-dependent than that in PSII. In WT-bRC, we observed significant coupling of ET with Glu-L212 protonation upon oxidation of the Fe complex and a dramatic E(m)(Fe) downshift by 230 mV upon formation of Q(A)(-) (but not Q(B)(-)) due to the absence of proton uptake of Glu-L212. Changes in net charges of the His ligands of the Fe complex appear to be the nature of the redox event if we assume the involvement of the Fe complex in the ET.
Ishikita
Hiroshi
H
Institute of Chemistry and Biochemistry, Free University of Berlin, Takustrasse 6, D-14195, Berlin, Germany. hzi1@usc.edu
Galstyan
Artur
A
Knapp
Ernst-Walter
EW
D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D004579:Electron Transport; D006863:Hydrogen-Ion Concentration; D007501:Iron / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D008958:Models, Molecular; D015394:Molecular Structure; D019159:Nonheme Iron Proteins / Q000737:chemistry* / Q000378:metabolism; D010084:Oxidation-Reduction; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000378:metabolism; D011522:Protons; D012242:Rhodobacter sphaeroides / Q000378:metabolism*
D000596:Amino Acids; D001426:Bacterial Proteins; D019159:Nonheme Iron Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D011522:Protons; D007501:Iron