Evidence map›Paper›PMID 35796895›Full record

ArticleOrigins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life2022

Competitive interaction of Mn(II) and Fe(II) cations with the high-affinity Mn-binding site of the photosystem II: evolutionary aspect.

E R Lovyagina, B К Semin

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Article in Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 58% of its field
1 · What the graph read from it

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3 · Its place in the literature

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0 citing papers in PubMed, 1 citations in OpenAlex.

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4 · The record

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5 · Who and what money

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2 authors at 1 institution in 1 country.

E R LovyaginaDepartment of Biophysics, Faculty of Biology, Lomonosov Moscow State University, 119234, Moscow, Russia.
B К SeminDepartment of Biophysics, Faculty of Biology, Lomonosov Moscow State University, 119234, Moscow, Russia. seminbk@mail.ru.
Lomonosov Moscow State University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The evolutionary origin of the oxygen-evolving complex (OEC) in the photosystem II (PSII) is still unclear, as is the nature of electron source for the photosystem before the OEC had appeared. Johnson et al. (in PNAS 110:11238, 2013) speculated that Mn(II) cations were the source of electrons for transitional photosystems. However, Archean oceans also contained Fe(II) cations at concentrations comparable or higher than that of Mn(II). Fe(II) cations can bind to the high-affinity (НА) Mn-binding site in the OEC (Semin et al. in Biochemistry 41:5854, 2002). Now we have investigated the competitive interaction of Mn(II) and Fe(II) cations with the HA site in the Mn-depleted PSII membranes (PSII[-Mn]). Fe cations, oxidized under illumination, bind strongly to the HA site and, thus, prevent the interaction of Mn(II) with this site. If the Mn(II) and Fe(II) cations, at relatively equal concentration, are simultaneously present in the buffer, together with PSII(-Mn) membranes, there is competition between these two cations for the binding site, which manifests itself in partial inhibition of the Mn(II) oxidation and the blocking of the HA site by Fe(II) cations. If the concentration of Fe(II) cations is several times higher than the concentration of Mn(II), the HA site is completely blocked and the oxidation of Mn(II) cations is inhibited; under saturating light, the effectiveness of this inhibitory effect increases. This may be due to the generation of H

Indexed as

ManganesePhotosystem II Protein ComplexBinding SitesCationsElectron TransportFerrous CompoundsHydrogen PeroxideIronOxidation-ReductionOxygenSpinacia oleraceaCationsFerrous CompoundsHydrogen PeroxideIronManganeseOxygenPhotosystem II Protein ComplexEvolutionFerrous ironManganeseMn-binding high-affinity sitePhotosystem II

Identifiers

PMID35796895
OpenAlexW4284680274

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