Methionine oxidation and its effect on the stability of a reconstituted subunit of the light-harvesting complex from Rhodospirillum rubrum. 2001

Z Y Wang, and M Shimonaga, and Y Muraoka, and M Kobayashi, and T Nozawa
Department of Biomolecular Engineering, Faculty of Engineering, Center for Interdisciplinary Research, Tohoku University, Sendai, Japan. wang@biophys.che.tohoku.ac.jp

An additional component in the purified core light-harvesting complex (LH1) from wild-type purple photosynthetic bacterium Rhodospirillum rubrum has been identified as an oxidized species of alpha-polypeptide by MALDI-TOF mass spectrometry. This component appears as a slightly earlier-eluting peak in the RP-HPLC chromatogram compared with the authentic alpha-polypeptide. The oxidation site has been determined to be the N-terminal methionine residue by high-resolution NMR spectroscopy, where the methionine is oxidized to methionine sulfoxide in a diastereoisomeric form. Interconversion between the oxidized and authentic alpha-polypeptides has been confirmed by selective oxidation and reduction. The oxidative modification of methionine is shown to have discernible effects on the ability to form B820 subunit with beta-polypeptide and bacteriochlorophyll a, and on the stability of the reconstituted B820 subunit. Both the ability and the stability for the samples using the oxidized alpha-polypeptide are moderately reduced, indicating that the oxidation-induced conformational change in the N-terminal domain of alpha-polypeptide may affect the pigment-binding environment through a long-range interaction. The MALDI-TOF mass results also reveal that the N-terminus of alpha-polypeptide is formylated and no phosphorylation has occurred in this polypeptide.

UI MeSH Term Description Entries
D008715 Methionine A sulfur-containing essential L-amino acid that is important in many body functions. L-Methionine,Liquimeth,Methionine, L-Isomer,Pedameth,L-Isomer Methionine,Methionine, L Isomer
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D002851 Chromatography, High Pressure Liquid Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed. Chromatography, High Performance Liquid,Chromatography, High Speed Liquid,Chromatography, Liquid, High Pressure,HPLC,High Performance Liquid Chromatography,High-Performance Liquid Chromatography,UPLC,Ultra Performance Liquid Chromatography,Chromatography, High-Performance Liquid,High-Performance Liquid Chromatographies,Liquid Chromatography, High-Performance
D012247 Rhodospirillum rubrum Vibrio- to spiral-shaped phototrophic bacteria found in stagnant water and mud exposed to light.
D045322 Photosynthetic Reaction Center Complex Proteins Protein complexes that take part in the process of PHOTOSYNTHESIS. They are located within the THYLAKOID MEMBRANES of plant CHLOROPLASTS and a variety of structures in more primitive organisms. There are two major complexes involved in the photosynthetic process called PHOTOSYSTEM I and PHOTOSYSTEM II. Photosynthetic Complex,Photosynthetic Reaction Center,Photosynthetic Reaction Center Complex Protein,Photosynthetic Complexes,Photosynthetic Reaction Centers,Center, Photosynthetic Reaction,Complex, Photosynthetic,Complexes, Photosynthetic,Reaction Center, Photosynthetic,Reaction Centers, Photosynthetic
D045342 Light-Harvesting Protein Complexes Complexes containing CHLOROPHYLL and other photosensitive molecules. They serve to capture energy in the form of PHOTONS and are generally found as components of the PHOTOSYSTEM I PROTEIN COMPLEX or the PHOTOSYSTEM II PROTEIN COMPLEX. Antenna Complexes, Light-Harvesting,Light-Harvesting Antenna Complexes,Light-Harvesting Chlorophyll Protein,Light-Harvesting Chlorophyll Protein Complexes,Antenna Complexes, Light Harvesting,Chlorophyll Protein, Light-Harvesting,Complexes, Light-Harvesting Antenna,Complexes, Light-Harvesting Protein,Light Harvesting Antenna Complexes,Light Harvesting Chlorophyll Protein,Light Harvesting Chlorophyll Protein Complexes,Light Harvesting Protein Complexes,Protein Complexes, Light-Harvesting
D019032 Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization A mass spectrometric technique that is used for the analysis of large biomolecules. Analyte molecules are embedded in an excess matrix of small organic molecules that show a high resonant absorption at the laser wavelength used. The matrix absorbs the laser energy, thus inducing a soft disintegration of the sample-matrix mixture into free (gas phase) matrix and analyte molecules and molecular ions. In general, only molecular ions of the analyte molecules are produced, and almost no fragmentation occurs. This makes the method well suited for molecular weight determinations and mixture analysis. Laser Desorption-Ionization Mass Spectrometry, Matrix-Assisted,MALD-MS,MALDI,Mass Spectrometry, Matrix-Assisted Laser Desorption-Ionization,Mass Spectroscopy, Matrix-Assisted Laser Desorption-Ionization,Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry,Spectroscopy, Mass, Matrix-Assisted Laser Desorption-Ionization,MALDI-MS,MS-MALD,SELDI-TOF-MS,Surface Enhanced Laser Desorption Ionization Mass Spectrometry,Laser Desorption Ionization Mass Spectrometry, Matrix Assisted,MALDI MS,Mass Spectrometry, Matrix Assisted Laser Desorption Ionization,Mass Spectroscopy, Matrix Assisted Laser Desorption Ionization,Matrix Assisted Laser Desorption Ionization Mass Spectrometry
D019906 Nuclear Magnetic Resonance, Biomolecular NMR spectroscopy on small- to medium-size biological macromolecules. This is often used for structural investigation of proteins and nucleic acids, and often involves more than one isotope. Biomolecular Nuclear Magnetic Resonance,Heteronuclear Nuclear Magnetic Resonance,NMR Spectroscopy, Protein,NMR, Biomolecular,NMR, Heteronuclear,NMR, Multinuclear,Nuclear Magnetic Resonance, Heteronuclear,Protein NMR Spectroscopy,Biomolecular NMR,Heteronuclear NMR,Multinuclear NMR,NMR Spectroscopies, Protein,Protein NMR Spectroscopies,Spectroscopies, Protein NMR,Spectroscopy, Protein NMR

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