T Y Fufina

Summary

Country: Russia

Publications

  1. ncbi request reprint Examination of stability of mutant photosynthetic reaction center of Rhodobacter sphaeroides I(L177)H and determination of location of bacteriochlorophyll covalently bound to the protein
    T Y Fufina
    Institute of Basic Biological Problems, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia
    Biochemistry (Mosc) 75:208-13. 2010
  2. pmc Expression, purification, crystallization and preliminary X-ray structure analysis of wild-type and L(M196)H-mutant Rhodobacter sphaeroides reaction centres
    A G Gabdulkhakov
    Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russian Federation
    Acta Crystallogr Sect F Struct Biol Cryst Commun 69:506-9. 2013
  3. doi request reprint The site-directed mutation I(L177)H in Rhodobacter sphaeroides reaction center affects coordination of P(A) and B(B) bacteriochlorophylls
    L G Vasilieva
    Institute of Basic Biological Problems, Russian Academy of Sciences, Pushchino, Moscow, Russia
    Biochim Biophys Acta 1817:1407-17. 2012
  4. ncbi request reprint Mutant reaction centers of Rhodobacter sphaeroides I(L177)H with strongly bound bacteriochlorophyll a: structural properties and pigment-protein interactions
    A A Zabelin
    Institute of Basic Biological Problems, Pushchino, Moscow Region, 142290, Russia
    Biochemistry (Mosc) 74:68-74. 2009
  5. doi request reprint Different effects of identical symmetry-related mutations near the bacteriochlorophyll dimer in the photosynthetic reaction center of Rhodobacter sphaeroides
    L G Vasilieva
    Institute of Basic Problems of Biology, Pushchino, Moscow Region, 142290, Russia
    Biochemistry (Mosc) 80:647-53. 2015
  6. ncbi request reprint Substitution of isoleucine L177 by histidine affects the pigment composition and properties of the reaction center of the purple bacterium Rhodobacter sphaeroides
    R A Khatypov
    Institute of Basic Biological Problems, Pushchino, Moscow Region, 142290, Russia
    Biochemistry (Mosc) 70:1256-61. 2005

Collaborators

  • M M Leonova
  • V A Shkuropatova
  • L G Vasilieva
  • V A Shuvalov
  • A G Gabdulkhakov
  • R A Khatypov
  • A A Zabelin
  • U Mueller
  • M G Zvereva
  • A Y Shkuropatov
  • T I Bolgarina

Detail Information

Publications6

  1. ncbi request reprint Examination of stability of mutant photosynthetic reaction center of Rhodobacter sphaeroides I(L177)H and determination of location of bacteriochlorophyll covalently bound to the protein
    T Y Fufina
    Institute of Basic Biological Problems, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia
    Biochemistry (Mosc) 75:208-13. 2010
    ..Spectral properties of the BChl covalently bound with the protein in I(L177)H RC do not change. The results demonstrate that BChl P(A) is the molecule of BChl tightly bound with the L-subunit in mutant RC as it was supposed earlier...
  2. pmc Expression, purification, crystallization and preliminary X-ray structure analysis of wild-type and L(M196)H-mutant Rhodobacter sphaeroides reaction centres
    A G Gabdulkhakov
    Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russian Federation
    Acta Crystallogr Sect F Struct Biol Cryst Commun 69:506-9. 2013
    ....
  3. doi request reprint The site-directed mutation I(L177)H in Rhodobacter sphaeroides reaction center affects coordination of P(A) and B(B) bacteriochlorophylls
    L G Vasilieva
    Institute of Basic Biological Problems, Russian Academy of Sciences, Pushchino, Moscow, Russia
    Biochim Biophys Acta 1817:1407-17. 2012
    ..This article is part of a Special Issue entitled: Photosynthesis Research for Sustainability: from Natural to Artificial...
  4. ncbi request reprint Mutant reaction centers of Rhodobacter sphaeroides I(L177)H with strongly bound bacteriochlorophyll a: structural properties and pigment-protein interactions
    A A Zabelin
    Institute of Basic Biological Problems, Pushchino, Moscow Region, 142290, Russia
    Biochemistry (Mosc) 74:68-74. 2009
    ..Structural changes are observed in the monomer bacteriochlorophyll B(B) binding site in the inactive chromophore branch of the mutant RCs...
  5. doi request reprint Different effects of identical symmetry-related mutations near the bacteriochlorophyll dimer in the photosynthetic reaction center of Rhodobacter sphaeroides
    L G Vasilieva
    Institute of Basic Problems of Biology, Pushchino, Moscow Region, 142290, Russia
    Biochemistry (Mosc) 80:647-53. 2015
    ..We suggest that the mutation I(M206)H and substitution of amino acid residues in M203-M205 positions could disturb glycolipid binding on the RC surface near BChl BA that is important for stable assembly of the complex in the membrane. ..
  6. ncbi request reprint Substitution of isoleucine L177 by histidine affects the pigment composition and properties of the reaction center of the purple bacterium Rhodobacter sphaeroides
    R A Khatypov
    Institute of Basic Biological Problems, Pushchino, Moscow Region, 142290, Russia
    Biochemistry (Mosc) 70:1256-61. 2005
    ....