Specific Ca2+-binding motif in the LH1 complex from photosynthetic bacterium Thermochromatium tepidum as revealed by optical spectroscopy and structural modeling

Fei Ma, Yukihiro Kimura, Long-Jiang Yu, Peng Wang, Xi Cheng Ai, Zheng Yu Wang, Jian Ping Zhang

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

Native and Ca2+-depleted light-harvesting-reaction center core complexes (LH1-RC) from the photosynthetic bacterium Thermochromatium (Tch.) tepidum exhibit maximal LH1-Qy absorption at 915 and 889 nm, respectively. To understand the structural origins of the spectral variation, we performed spectroscopic and structure modeling investigations. For the 889 nm form of LH1-RC, bacteriochlorophyll a (BChl a) in the native form was found by means of near-infrared Fourier-transform Raman spectroscopy, a higher degree of macrocycle distortion and a stronger hydrogen bond with the β-Trp -8 residue. SWISS-MODEL structure modeling suggests the presence of a specific coordination motif of Ca2+ at the C-terminus of the α-subunit of LH1, while MODELLER reveals the tilt of α- and β-polypeptides with reference to the structural template, as well as a change in the concentric orientation of BChl a molecules, both of which may be connected to the long-wavelength LH1-Qy absorption of the 915 nm form. The carotenoid spirilloxanthin shows a twisted all-trans configuration in both forms of LH1 as evidenced by the resonance Raman spectroscopic results. With regard to the thermal stability, the 915 nm form was shown by the use of temperature-dependent fluorescence spectroscopy to be approximately 20 K more stable than the 889 nm form, which may be ascribed to the specific Ca 2+-binding motif of LH1.

Original languageEnglish
Pages (from-to)1739-1749
Number of pages11
JournalFEBS Journal
Volume276
Issue number6
DOIs
Publication statusPublished - Mar 2009
Externally publishedYes

Fingerprint

Photosynthetic Reaction Center Complex Proteins
Bacteriochlorophylls
Spectrum Analysis
Bacteria
Raman Spectrum Analysis
Fluorescence Spectrometry
Fluorescence spectroscopy
Fourier Analysis
Carotenoids
Raman spectroscopy
Hydrogen
Fourier transforms
Hydrogen bonds
Thermodynamic stability
Hot Temperature
Infrared radiation
Light
Wavelength
Peptides
Molecules

Keywords

  • 3D structural modeling
  • Light-harvesting-reaction center core complex (LH1-RC)
  • Photosynthetic purple bacterium
  • Raman spectroscopy
  • Thermochromatium (Tch.) tepidum

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology
  • Medicine(all)

Cite this

Specific Ca2+-binding motif in the LH1 complex from photosynthetic bacterium Thermochromatium tepidum as revealed by optical spectroscopy and structural modeling. / Ma, Fei; Kimura, Yukihiro; Yu, Long-Jiang; Wang, Peng; Ai, Xi Cheng; Wang, Zheng Yu; Zhang, Jian Ping.

In: FEBS Journal, Vol. 276, No. 6, 03.2009, p. 1739-1749.

Research output: Contribution to journalArticle

Ma, Fei ; Kimura, Yukihiro ; Yu, Long-Jiang ; Wang, Peng ; Ai, Xi Cheng ; Wang, Zheng Yu ; Zhang, Jian Ping. / Specific Ca2+-binding motif in the LH1 complex from photosynthetic bacterium Thermochromatium tepidum as revealed by optical spectroscopy and structural modeling. In: FEBS Journal. 2009 ; Vol. 276, No. 6. pp. 1739-1749.
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abstract = "Native and Ca2+-depleted light-harvesting-reaction center core complexes (LH1-RC) from the photosynthetic bacterium Thermochromatium (Tch.) tepidum exhibit maximal LH1-Qy absorption at 915 and 889 nm, respectively. To understand the structural origins of the spectral variation, we performed spectroscopic and structure modeling investigations. For the 889 nm form of LH1-RC, bacteriochlorophyll a (BChl a) in the native form was found by means of near-infrared Fourier-transform Raman spectroscopy, a higher degree of macrocycle distortion and a stronger hydrogen bond with the β-Trp -8 residue. SWISS-MODEL structure modeling suggests the presence of a specific coordination motif of Ca2+ at the C-terminus of the α-subunit of LH1, while MODELLER reveals the tilt of α- and β-polypeptides with reference to the structural template, as well as a change in the concentric orientation of BChl a molecules, both of which may be connected to the long-wavelength LH1-Qy absorption of the 915 nm form. The carotenoid spirilloxanthin shows a twisted all-trans configuration in both forms of LH1 as evidenced by the resonance Raman spectroscopic results. With regard to the thermal stability, the 915 nm form was shown by the use of temperature-dependent fluorescence spectroscopy to be approximately 20 K more stable than the 889 nm form, which may be ascribed to the specific Ca 2+-binding motif of LH1.",
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AU - Ai, Xi Cheng

AU - Wang, Zheng Yu

AU - Zhang, Jian Ping

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AB - Native and Ca2+-depleted light-harvesting-reaction center core complexes (LH1-RC) from the photosynthetic bacterium Thermochromatium (Tch.) tepidum exhibit maximal LH1-Qy absorption at 915 and 889 nm, respectively. To understand the structural origins of the spectral variation, we performed spectroscopic and structure modeling investigations. For the 889 nm form of LH1-RC, bacteriochlorophyll a (BChl a) in the native form was found by means of near-infrared Fourier-transform Raman spectroscopy, a higher degree of macrocycle distortion and a stronger hydrogen bond with the β-Trp -8 residue. SWISS-MODEL structure modeling suggests the presence of a specific coordination motif of Ca2+ at the C-terminus of the α-subunit of LH1, while MODELLER reveals the tilt of α- and β-polypeptides with reference to the structural template, as well as a change in the concentric orientation of BChl a molecules, both of which may be connected to the long-wavelength LH1-Qy absorption of the 915 nm form. The carotenoid spirilloxanthin shows a twisted all-trans configuration in both forms of LH1 as evidenced by the resonance Raman spectroscopic results. With regard to the thermal stability, the 915 nm form was shown by the use of temperature-dependent fluorescence spectroscopy to be approximately 20 K more stable than the 889 nm form, which may be ascribed to the specific Ca 2+-binding motif of LH1.

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