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Molecular interfere...
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Sigfridsson Clauss, KajsaLund University,Lunds universitet,MAX IV-laboratoriet,MAX IV Laboratory
(författare)
Molecular interference of Cd2+ with Photosystem II
- Artikel/kapitelEngelska2004
Förlag, utgivningsår, omfång ...
Nummerbeteckningar
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LIBRIS-ID:oai:lup.lub.lu.se:e165ed32-fabc-43e7-b058-c32cdbf9b7be
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https://lup.lub.lu.se/record/138662URI
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https://doi.org/10.1016/j.bbabio.2004.07.003DOI
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Språk:engelska
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Sammanfattning på:engelska
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Ämneskategori:art swepub-publicationtype
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Ämneskategori:ref swepub-contenttype
Anmärkningar
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Many heavy metals inhibit electron transfer reactions in Photosystem II (PSII). Cd2+ is known to exchange, with high affinity in a slow reaction, for the Ca2+ cofactor in the Ca/Mn cluster that constitutes the oxygen-evolving center. This results in inhibition of photosynthetic oxygen evolution. There are also indications that Cd2+ binds to other sites in PSII, potentially to proton channels in analogy to heavy metal binding in photosynthetic reaction centers from purple bacteria. In search for the effects of Cd2+-binding to those sites, we have studied how Cd2+ affects electron transfer reactions in PSII after short incubation times and in sites, which interact with Cd2+ with low affinity. Overall electron transfer and partial electron transfer were studied by a combination of EPR spectroscopy of individual redox components, flash-induced variable fluorescence and steady state oxygen evolution measurements. Several effects of Cd2+ were observed: (i) the amplitude of the flash-induced variable fluorescence was lost indicating that electron transfer from Y-Z to P-680(+) was inhibited; (ii) Q(A)(-) to Q(B) electron transfer was slowed down; (iii) the S-2 state multiline EPR signal was not observable; (iv) steady state oxygen evolution was inhibited in both a high-affinity and a low-affinity site; (v) the spectral shape of the EPR signal from Q(A)(-)Fe(2+) was modified but its amplitude was not sensitive to the presence of Cd2+. In addition, the presence of both Ca2+ and DCMU abolished Cd2+-induced effects partially and in different sites. The number of sites for Cd2+ binding and the possible nature of these sites are discussed. (C) 2004 Elsevier B.V. All rights reserved.
Ämnesord och genrebeteckningar
Biuppslag (personer, institutioner, konferenser, titlar ...)
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Bernat, GaborLund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)biok-gbe
(författare)
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Mamedov, FikretLund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)biok-fma
(författare)
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Styring, StenbjörnLund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)biok-sst
(författare)
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Lunds universitetMAX IV-laboratoriet
(creator_code:org_t)
Sammanhörande titlar
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Ingår i:Biochimica et Biophysica Acta - Bioenergetics: Elsevier BV1659:1, s. 19-310005-2728
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