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Structural consequences of the replacement of glycine M203 with aspartic acid in the reaction center from Rhodobacter sphaeroides.

Fyfe PK, Ridge JP, McAuley KE, Cogdell RJ, Isaacs NW, Jones MR
Biochemistry 39 5953-60 (2000)
Related entries: 1mps, 1qov

Cited: 19 times
EuropePMC logo PMID: 10821666

Abstract

Reaction centers with the double mutation Phe M197 to Arg and Gly M203 to Asp (FM197R/GM203D) have been crystallized from an antenna-deficient strain of Rhodobacter sphaeroides, and the structure has been determined at 2.7 A resolution. Unlike in reaction centers with a single FM197R mutation, the Arg M197 residue in the FM197R/GM203D reaction center adopts a position similar to that of the native Phe residue in the wild-type reaction center. Asp M203 is packed in such a way that the gamma-carboxy group interacts with the backbone carbonyl of Arg M197. The Asp M203 residue takes up part of the volume that is occupied in the wild-type reaction center by a water molecule. This water has been proposed to form a hydrogen bond interaction with the 9-keto carbonyl group of the active branch accessory bacteriochlorophyll, particularly when the primary donor bacteriochlorophylls are oxidized. The GM203D mutation therefore appears to remove the possibility of this hydrogen bond interaction by exclusion of this water molecule, as well as altering the local dielectric environment of the 9-keto carbonyl group. We examine whether the observed structural changes can provide new or alternative explanations for the absorbance and electron-transfer properties of reaction centers with the FM197R and GM203D mutations.

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  2. Protein-lipid interactions in the purple bacterial reaction centre. Jones MR, Fyfe PK, Roszak AW, Isaacs NW, Cogdell RJ. Biochim. Biophys. Acta 1565 206-214 (2002)
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  1. Which side of the pi-macrocycle plane of (bacterio)chlorophylls is favored for binding of the fifth ligand? Oba T, Tamiaki H. Photosyn. Res. 74 1-10 (2002)
  2. B-branch electron transfer in reaction centers of Rhodobacter sphaeroides assessed with site-directed mutagenesis. de Boer AL, Neerken S, de Wijn R, Permentier HP, Gast P, Vijgenboom E, Hoff AJ. Photosyn. Res. 71 221-239 (2002)
  3. Alteration of protein structure induced by low-energy (<18 eV) electrons. I. The peptide and disulfide bridges. Abdoul-Carime H, Cecchini S, Sanche L. Radiat. Res. 158 23-31 (2002)
  4. Identification and assessment of cardiolipin interactions with E. coli inner membrane proteins. Corey RA, Song W, Duncan AL, Ansell TB, Sansom MSP, Stansfeld PJ. Sci Adv 7 eabh2217 (2021)
  5. Comparative analyses of three-dimensional models of bacterial reaction centers. Camara-Artigas A, Allen JP. Photosyn. Res. 81 227-237 (2004)
  6. Femtosecond charge separation in dry films of reaction centers of Rhodobacter sphaeroides and Chloroflexus aurantiacus. Yakovlev AG, Khmelnitsky AY, Shuvalov VA. Biochemistry Mosc. 77 444-455 (2012)
  7. Orientation and conformation of lipids in crystals of transmembrane proteins. Marsh D, Páli T. Eur. Biophys. J. 42 119-146 (2013)
  8. Temperature and cryoprotectant influence secondary quinone binding position in bacterial reaction centers. Pokkuluri PR, Laible PD, Crawford AE, Mayfield JF, Yousef MA, Ginell SL, Hanson DK, Schiffer M. FEBS Lett. 570 171-174 (2004)
  9. Characterization of protein matrix motions in the Rb. sphaeroides photosynthetic reaction center. Stoica I. J Mol Model 12 468-480 (2006)
  10. High pressure near infrared study of the mutated light-harvesting complex LH2. Braun P, Gebhardt R, Kwa L, Doster W. Braz. J. Med. Biol. Res. 38 1273-1278 (2005)
  11. Resonance Raman characterization of Rhodobacter capsulatus reaction centers with lysine mutations near the accessory bacteriochlorophylls. Chen L, Kirmaier C, Holten D, Bocian DF. Photosyn. Res. 83 35-43 (2005)
  12. Femtosecond stage of electron transfer in reaction centers of the triple mutant SL178K/GM203D/LM214H of Rhodobacter sphaeroides. Yakovlev AG, Shkuropatova TA, Shkuropatova VA, Shuvalov VA. Biochemistry Mosc. 75 412-422 (2010)
  13. Primary electron transfer in reaction centers of YM210L and YM210L/HL168L mutants of Rhodobacter sphaeroides. Yakovlev AG, Vasilieva LG, Khmelnitskaya TI, Shkuropatova VA, Shkuropatov AY, Shuvalov VA. Biochemistry Mosc. 75 832-840 (2010)
  14. Putative hydrogen bond to tyrosine M208 in photosynthetic reaction centers from Rhodobacter capsulatus significantly slows primary charge separation. Saggu M, Carter B, Zhou X, Faries K, Cegelski L, Holten D, Boxer SG, Kirmaier C. J Phys Chem B 118 6721-6732 (2014)


Related citations provided by authors (2)

  1. Structural details of an interaction between cardiolipin and an integral membrane protein.. McAuley KE, Fyfe PK, Ridge JP, Isaacs NW, Cogdell RJ, Jones MR Proc Natl Acad Sci U S A 96 14706-11 (1999)
  2. Structural studies of wild-type and mutant reaction centers from an antenna-deficient strain of Rhodobacter sphaeroides: monitoring the optical properties of the complex from bacterial cell to crystal.. McAuley-Hecht KE, Fyfe PK, Ridge JP, Prince SM, Hunter CN, Isaacs NW, Cogdell RJ, Jones MR Biochemistry 37 4740-50 (1998)

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