Substituting Fe for two of the four Mn ions in photosystem II—effects on water-oxidation

Journal of bioenergetics - Tập 48 - Trang 227-240 - 2016
Boris K. Semin1,2, Michael Seibert1
1BioEnergy Sciences & Technology Directorate, National Renewable Energy Laboratory, Golden, USA
2Department of Biophysics, Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia

Tóm tắt

We have investigated the interaction of Fe(II) cations with Ca-depleted PSII membranes (PSII[-Ca,4Mn]) in the dark and found that Fe(II) incubation removes 2 of 4 Mn ions from the tetranuclear Mn cluster of the photosynthetic O2-evolving complex (OEC). The reduction of Mn ions in PSII(-Ca,4Mn) by Fe(II) and the concomitant release of two Mn(II) cations is accompanied by the binding of newly generated Fe(III) in at least one vacated Mn site. Flash-induced chlorophyll (Chl) fluorescence yield measurements of this new 2Mn/nFe cluster (PSII[-Ca,2Mn,nFe]) show that charge recombination in the presence of 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU) occurs between Qa - and the remaining Mn/Fe cluster (but not YZ ●) in the OEC, and extraction of 2 Mn occurs uniformly in all PSII complexes. No O2 evolution is observed, but the heteronuclear metal cluster in PSII(-Ca,2Mn,nFe) samples is still able to supply electrons for reduction of the exogenous electron acceptor, 2,6-dichlorophrenolindophenol, by photooxidizing water and producing H2O2 in the absence of an exogenous donor as seen previously with PSII(-Ca,4Mn). Selective extraction of Mn or Fe cations from the 2Mn/nFe heteronuclear cluster demonstrates that the high-affinity Mn-binding site is occupied by one of the iron cations. It is notable that partial water-oxidation function still occurs when only two Mn cations are present in the PSII OEC.

Tài liệu tham khảo

Boussac A, Zimmermann J-L, Rutherford AW (1990) Factors influencing the formation of modified S2 EPR signal and the S3 EPR signal in Ca(2+)-depleted photosystem II. FEBS Lett 277:69–74

Ghanotakis DF, Topper JN, Yocum CF (1984b) Exogenous reductants reduce and destroy the Mn-complex in photosystem II membranes depleted of the 17 and 23 kDa polypeptides. Biochim Biophys Aсta 767:524–531

Jiang W, Yun D, Saleh L, Barr EW, Xing G, Hoffart LM, Maslak M-A, Krebs C, Bollinger JM Jr (2007) A manganese(IV)/iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase. Science 316:1188–1191

Ono T, Mino H (1999) Unique binding site for Mn2+ ion responsible for reducing an oxidized YZ tyrosine in manganese-depleted photosystem II membranes. Biochemistry 38:8778–8785

Peloquin JM, Campbell KA, Randall DW, Evanchik MA, Pecoraro VL, Armstrong WH, Britt RD (2000) 55Mn ENDOR of the S2-state multiline EPR signal of photosystem II: implications on the structure of the tetranuclear Mn cluster. J Am Chem Soc 122:10926–10942

Semin BK, Seibert M (2006a) Flash-induced blocking of the high-affinity, Mn-binding site by iron cations—dependence on the dark interval between flashes and binary oscillations of fluorescence yield. J Phys Chem B 110:25532–25542

Semin BK, Ghirardi ML, Seibert M (2002) Blocking of electron donation by Mn(II) to YZ • following incubation of Mn-depleted photosystem II membranes with Fe(II) in the light. Biochemistry 41:5854–5864