Effective binding of Tb3+ and La3+ cations on the donor side of Mn-depleted photosystem II
- PMID: 33146770
- DOI: 10.1007/s00775-020-01832-w
Effective binding of Tb3+ and La3+ cations on the donor side of Mn-depleted photosystem II
Abstract
The interaction of Tb3+ and La3+ cations with different photosystem II (PSII) membranes (intact PSII, Ca-depleted PSII (PSII[-Ca]) and Mn-depleted PSII (PSII[-Mn]) membranes) was studied. Although both lanthanide cations (Ln3+) interact only with Ca2+-binding site of oxygen-evolving complex (OEC) in PSII and PSII(-Ca) membranes, we found that in PSII(-Mn) membranes both Ln3+ ions tightly bind to another site localized on the oxidizing side of PSII. Binding of Ln3+ cations to this site is not protected by Ca2+ and is accompanied by very effective inhibition of Mn2+ oxidation at the high-affinity (HA) Mn-binding site ([Mn2+ + H2O2] couple was used as a donor of electrons). The values of the constant for inhibition of electron transport Ki are equal to 2.10 ± 0.03 µM for Tb3+ and 8.3 ± 0.4 µM for La3+, whereas OEC inhibition constant in the native PSII membranes is 323 ± 7 µM for Tb3+. The value of Ki for Tb3+ corresponds to Ki for Mn2+ cations in the reaction of diphenylcarbazide oxidation via HA site (1.5 µM) presented in the literature. Our results suggest that Ln3+ cations bind to the HA Mn-binding site in PSII(-Mn) membranes like Mn2+ or Fe2+ cations. Taking into account the fact that Mn2+ and Fe2+ cations bind to the HA site as trivalent cations after light-induced oxidation and the fact that Mn cation bound to the HA site (Mn4) is also in trivalent state, we can suggest that valency may be important for the interaction of Ln3+ with the HA site.
Keywords: Calcium; High-affinity Mn-binding site; Lanthanum; Oxygen-evolving complex; Photosystem II; Terbium.
Similar articles
-
Current analysis of cations substitution in the oxygen-evolving complex of photosystem II.Biophys Rev. 2024 Apr 30;16(2):237-247. doi: 10.1007/s12551-024-01186-6. eCollection 2024 Apr. Biophys Rev. 2024. PMID: 38737202 Free PMC article. Review.
-
Ca2+ effects on Fe(II) interactions with Mn-binding sites in Mn-depleted oxygen-evolving complexes of photosystem II and on Fe replacement of Mn in Mn-containing, Ca-depleted complexes.Photosynth Res. 2021 Feb;147(2):229-237. doi: 10.1007/s11120-020-00813-z. Epub 2021 Feb 2. Photosynth Res. 2021. PMID: 33532973
-
Blocking of electron donation by Mn(II) to Y(Z*) following incubation of Mn-depleted photosystem II membranes with Fe(II) in the light.Biochemistry. 2002 May 7;41(18):5854-64. doi: 10.1021/bi0200054. Biochemistry. 2002. PMID: 11980489
-
Competitive interaction of Mn(II) and Fe(II) cations with the high-affinity Mn-binding site of the photosystem II: evolutionary aspect.Orig Life Evol Biosph. 2022 Sep;52(1-3):113-128. doi: 10.1007/s11084-022-09625-8. Epub 2022 Jul 7. Orig Life Evol Biosph. 2022. PMID: 35796895
-
Reconstitution of the photosystem II Ca2+ binding site.Biochim Biophys Acta. 2004 Apr 12;1655(1-3):179-83. doi: 10.1016/j.bbabio.2003.08.012. Biochim Biophys Acta. 2004. PMID: 15100030 Review.
Cited by
-
Current analysis of cations substitution in the oxygen-evolving complex of photosystem II.Biophys Rev. 2024 Apr 30;16(2):237-247. doi: 10.1007/s12551-024-01186-6. eCollection 2024 Apr. Biophys Rev. 2024. PMID: 38737202 Free PMC article. Review.
References
-
- Umena Y, Kawakami K, Shen J-R, Kamiya N (2011) Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å. Nature 473:55–60. https://doi.org/10.1038/nature09913 - DOI - PubMed
-
- Najafpour MM, Renger G, Hołyńska M, Moghaddam AN, Aro EM, Carpentier R, Nishihara H, Eaton-Rye JJ, Shen J-R, Allakhverdiev SI (2016) Manganese compounds as water-oxidizing catalysts: from the natural water-oxidizing complex to nanosized manganese oxide structures. Chem Rev 116:2886–2936. https://doi.org/10.1021/acs.chemrev.5b00340 - DOI - PubMed
-
- Suga M, Akita F, Hirata K, Ueno G, Murakami H, Nakajima Y, Shimizu T, Yamashita K, Yamamoto M, Ago H, Shen J-R (2015) Native structure of photosystem II at 1.95 Å resolution viewed by femtosecond X-ray pulses. Nature 517:99–103. https://doi.org/10.1038/nature13991 - DOI - PubMed
-
- Young ID, Ibrahim M, Chatterjee R, Gul S, Fuller FD, Koroidov S, Brewster AS, Tran R, Alonso-Mori R, Kroll T, Michels-Clark T, Laksmono H, Sierra RG, Stan CA, Hussein R, Zhang M, Douthit L, Kubin M, de Lichtenberg C, Pham LV, Nilsson H, Cheah MH, Shevela D, Saracini C, Bean MA, Seuffert I, Sokaras D, Weng TC, Pastor E, Weninger C, Fransson T, Lassalle L, Brauer P, Aller P, Docker PT, Andi B, Orville AM, Glownia JM, Nelson S, Sikorski M, Zhu DL, Hunter MS, Lane TJ, Aquila A, Koglin JE, Robinson J, Liang MN, Boutet S, Lyubimov AY, Uervirojnangkoorn M, Moriarty NW, Liebschner D, Afonine PV, Waterman DG, Evans G, Wernet P, Dobbek H, Weis WI, Brunger AT, Zwart PH, Adams PD, Zouni A, Messinger J, Bergmann U, Sauter NK, Kern J, Yachandra VK, Yano J (2016) Structure of photosystem II and substrate binding at room temperature. Nature 540:453–457. https://doi.org/10.1038/nature20161 - DOI - PubMed - PMC
-
- Zhang M, Bommer M, Chatterjee R, Hussein R, Yano J, Dau H, Kern J, Dobbek H, Zouni A (2017) Structural insights into the light-driven auto-assembly process of the water-oxidizing Mn4CaO5-cluster in photosystem II. eLife 6:e26933. https://doi.org/10.7554/eLife.26933
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Miscellaneous