Rainer Hienerwadel

ORCID: 0000-0002-8059-7956
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About
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Research Areas
  • Photosynthetic Processes and Mechanisms
  • Spectroscopy and Quantum Chemical Studies
  • Photoreceptor and optogenetics research
  • Light effects on plants
  • Metal-Catalyzed Oxygenation Mechanisms
  • Metalloenzymes and iron-sulfur proteins
  • Microbial Fuel Cells and Bioremediation
  • Hemoglobin structure and function
  • Algal biology and biofuel production
  • Mitochondrial Function and Pathology
  • Antioxidant Activity and Oxidative Stress
  • Porphyrin and Phthalocyanine Chemistry
  • Microbial Community Ecology and Physiology
  • Electrochemical Analysis and Applications
  • Wastewater Treatment and Nitrogen Removal
  • Enzyme Structure and Function
  • Porphyrin Metabolism and Disorders
  • Chemical Analysis and Environmental Impact
  • Enzyme Catalysis and Immobilization
  • Cancer Research and Treatments
  • Protist diversity and phylogeny
  • Plant Stress Responses and Tolerance
  • X-ray Spectroscopy and Fluorescence Analysis
  • Free Radicals and Antioxidants
  • Marine and coastal ecosystems

Institut de Biosciences et Biotechnologies
2019-2023

Aix-Marseille Université
2005-2023

Commissariat à l'Énergie Atomique et aux Énergies Alternatives
2004-2021

CEA Cadarache
2020-2021

Centre National de la Recherche Scientifique
1996-2019

Institute of Environmental Biology and Biotechnology
2012

Centre de Gestion Scientifique
2009

University of Groningen
2007

Instituto di Biofisica
2007

CEA Paris-Saclay
1992-2001

Light makes light work of fatty acids Photosynthetic organisms are notable for their ability to capture energy and use it power biosynthesis. Some algae have gone a step beyond photosynthesis can initiate enzymatic photodecarboxylation acids, producing long-chain hydrocarbons. To understand this transformation, Sorigué et al. brought bear an array structural, computational, spectroscopic techniques fully characterized the catalytic cycle enzyme. These experiments consistent with mechanism...

10.1126/science.abd5687 article EN Science 2021-04-09

In oxygenic photosynthetic organisms, chlorophyll triplets are harmful excited states readily reacting with molecular oxygen to yield the reactive species (ROS) singlet oxygen. Carotenoids have a photoprotective role in membranes by preventing photoxidative damage through quenching of singlets and triplets. this work we used mutation analysis investigate architecture triplet sites within Lhcb5, monomeric antenna protein Photosystem II. The carotenoid formation as well production ROS...

10.1021/jp402977y article EN The Journal of Physical Chemistry B 2013-06-20

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTBicarbonate binding to the non-heme iron of photosystem II, investigated by Fourier transform infrared difference spectroscopy and 13C-labeled bicarbonate.Rainer Hienerwadel Catherine BerthomieuCite this: Biochemistry 1995, 34, 50, 16288–16297Publication Date (Print):December 19, 1995Publication History Published online1 May 2002Published inissue 19 December...

10.1021/bi00050a008 article EN Biochemistry 1995-12-01

The TyrZ•/TyrZ FTIR difference spectrum is reported for the first time in Mn-depleted photosystem II (PS II)-enriched membranes of spinach, PS core complexes Synechocystis sp. PCC 6803 WT, and mutant lacking TyrD (D2-Tyr160Phe). In Synechocystis, ν7'a(CO) δ(COH) infrared modes TyrZ are proposed to account at 1279 1255 cm-1. frequency these indicate that protonated pH 6 involved a strong hydrogen bond side chain histidine, probably D1-His190. A positive signal 1512 cm-1 assigned ν(CO) mode...

10.1021/bi980788m article EN Biochemistry 1998-07-01

Tyrosine D (TyrD), a side path electron carrier of photosystem II (PS II), has been studied by light-induced Fourier transform infrared (FTIR) difference spectroscopy in PS core complexes Synechocystis sp. PCC 6803 using the experimental conditions previously optimized to generate pure TyrD./TyrD FTIR spectrum II-enriched membranes spinach [Hienerwadel, R., Boussac, A., Breton, J., and Berthomieu, C. (1996) Biochemistry 35, 115447-115460]. IR modes TyrD TyrD. have identified specific 2H- or...

10.1021/bi971521a article EN Biochemistry 1997-12-01

The Escherichia coli ChrR enzyme is an obligatory two-electron quinone reductase that has many applications, such as in chromate bioremediation. Its crystal structure, solved at 2.2 Å resolution, shows it belongs to the flavodoxin superfamily which flavin mononucleotide (FMN) firmly anchored protein. crystallized a tetramer, and size exclusion chromatography showed this oligomeric form catalyzes reduction. Within dimers interact by pair of two hydrogen bond networks, each involving Tyr128...

10.1371/journal.pone.0036017 article EN cc-by PLoS ONE 2012-04-27

Abstract Background Photosystems are composed of two moieties, a reaction center and peripheral antenna system. In photosynthetic eukaryotes the latter system is proteins belonging to Lhc family. An increasing set evidences demonstrated how these polypeptides play relevant physiological function in both light harvesting photoprotection. Despite sequence similarity between associated with Photosystems, present knowledge on their role mostly limited complexes Photosystem II. Results this work...

10.1186/1471-2229-9-71 article EN cc-by BMC Plant Biology 2009-06-09

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTProtonation of Glu L212 following QB- Formation in the Photosynthetic Reaction Center Rhodobacter sphaeroides: Evidence from Time-Resolved Infrared SpectroscopyR. Hienerwadel, S. Grzybek, C. Fogel, W. Kreutz, M. Y. Okamura, L. Paddock, J. Breton, E. Nabedryk, and MaenteleCite this: Biochemistry 1995, 34, 9, 2832–2843Publication Date (Print):March 7, 1995Publication History Published online1 May 2002Published inissue 7 March...

10.1021/bi00009a013 article EN Biochemistry 1995-03-07

CP24 is a minor antenna complex of Photosystem II, which specific for land plants. It has been proposed that this involved in the process excess energy dissipation, protects plants from photodamage high light conditions. Here, we have investigated functional architecture complex, integrating mutation analysis with time-resolved spectroscopy. A comprehensive picture obtained about nature, spectroscopic properties, and role quenching solution pigments individual binding sites. The lowest...

10.1074/jbc.m109.036376 article EN cc-by Journal of Biological Chemistry 2009-08-22

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTFourier Transform Infrared Difference Spectroscopy of Secondary Quinone Acceptor Photoreduction in Proton Transfer Mutants Rhodobacter sphaeroidesE. Nabedryk, J. Breton, R. Hienerwadel, C. Fogel, W. Maentele, M. L. Paddock, and Y. OkamuraCite this: Biochemistry 1995, 34, 45, 14722–14732Publication Date (Print):November 1, 1995Publication History Published online1 May 2002Published inissue 1 November...

10.1021/bi00045a013 article EN Biochemistry 1995-11-01

The non heme iron environment of photosystem II is studied by light-induced infrared spectroscopy. A conclusion previous work [Hienerwadel, R., and Berthomieu, C. (1995) Biochemistry 34, 16288−16297] that bicarbonate a bidendate ligand the reduced monodentate in Fe3+ state. In this work, effects replacement with lactate, glycolate, glyoxylate, o-phenanthroline binding are investigated to determine specific interactions protein. Fe2+/Fe3+ FTIR spectra recorded 12C- 13C1-labeled lactate...

10.1021/bi002236l article EN Biochemistry 2001-03-08

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTTime-resolved infrared spectroscopy of electron transfer in bacterial photosynthetic reaction centers: dynamics binding and interaction upon QA QB reductionR. Hienerwadel, D. Thibodeau, F. Lenz, E. Nabedryk, J. Breton, W. Kreutz, MaenteleCite this: Biochemistry 1992, 31, 25, 5799–5808Publication Date (Print):June 30, 1992Publication History Published online1 May 2002Published inissue 30 June...

10.1021/bi00140a016 article EN Biochemistry 1992-06-30

In this work, the spectroscopic characteristics of carotenoids associated with antenna complexes Photosystem I have been studied. Pigment composition, absorption spectra, and laser-induced triplet-minus-singlet (T−S) spectra were determined for native LHCI from wild type (WT) lut2 mutant Arabidopsis thaliana as well reconstituted individual Lhca WT mutated complexes. All bind lutein violaxanthin, while β-carotene was found to be only preparation recombinant Lhca3. complexes, main bands are...

10.1021/bi602531k article EN Biochemistry 2007-02-28

Two redox active tyrosines are present in the homologous polypeptides D1 and D2 of photosystem II (PS II). TyrZ (D1−161) is involved electron transfer reactions resulting oxygen evolution, while TyrD (D2−160) usually forms a dark-stable radical. In Mn-depleted PS II, TyrD• can be slowly reduced by exogenous reductants. Charge separation then results oxidation reduction primary acceptor QA. The semiquinone QA- reoxidized oxidants like ferricyanide. work, experimental conditions leading to...

10.1021/bi961952d article EN Biochemistry 1996-01-01

The redox active tyrosines, YZ and YD, of Photosystem II are oxidized by P680+ to the neutral radical. Such oxidation requires coupling electron transfer phenolic proton. Studies multiphasic kinetics in Mn-depleted PSII core complexes have shown that relative amplitudes kinetic components pH-dependent with one component showing a t1/2 microsecond tens range (pH 4–8). Sjödin coworkers (M. Sjödin, S. Styring, B. Åkemark, L. Sun Hammarström, Philos. Trans. R. Soc. London, Ser. B, 2002, 357,...

10.1039/b407423h article EN Physical Chemistry Chemical Physics 2004-01-01

The cytochrome bound to the photosynthetic reaction center of Rhodovulum sulfidophilum presents two unusual characteristics with respect well characterized tetraheme cytochromes. This contains only three hemes because it lacks peptide motif CXXCH, which binds most distal fourth heme. In addition, we show that sixth axial ligand third heme is a cysteine (Cys-148) instead usual methionine ligand. exchange results in very low midpoint potential (–160 ± 10 mV). influence on this was further...

10.1074/jbc.m400361200 article EN cc-by Journal of Biological Chemistry 2004-06-01
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