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Strong effects of an individual water molecule on the rate of light-driven charge separation in the Rhodobacter sphaeroides reaction center.

Potter JA, Fyfe PK, Frolov D, Wakeham MC, van Grondelle R, Robert B, Jones MR
J Biol Chem 280 27155-64 (2005)
Cited: 20 times
EuropePMC logo PMID: 15908429

Abstract

The role of a water molecule (water A) located between the primary electron donor (P) and first electron acceptor bacteriochlorophyll (B(A)) in the purple bacterial reaction center was investigated by mutation of glycine M203 to leucine (GM203L). The x-ray crystal structure of the GM203L reaction center shows that the new leucine residue packs in such a way that water A is sterically excluded from the complex, but the structure of the protein-cofactor system around the mutation site is largely undisturbed. The results of absorbance and resonance Raman spectroscopy were consistent with either the removal of a hydrogen bond interaction between water A and the keto carbonyl group of B(A) or a change in the local electrostatic environment of this carbonyl group. Similarities in the spectroscopic properties and x-ray crystal structures of reaction centers with leucine and aspartic acid mutations at the M203 position suggested that the effects of a glycine to aspartic acid substitution at the M203 position can also be explained by steric exclusion of water A. In the GM203L mutant, loss of water A was accompanied by an approximately 8-fold slowing of the rate of decay of the primary donor excited state, indicating that the presence of water A is important for optimization of the rate of primary electron transfer. Possible functions of this water molecule are discussed, including a switching role in which the redox potential of the B(A) acceptor is rapidly modulated in response to oxidation of the primary electron donor.

Articles - 2boz mentioned but not cited (2)

  1. 'Double water exclusion': a hypothesis refining the O-ring theory for the hot spots at protein interfaces. Li J, Liu Q. Bioinformatics 25 743-750 (2009)
  2. Directed evolution and in silico analysis of reaction centre proteins reveal molecular signatures of photosynthesis adaptation to radiation pressure. Rea G, Lambreva M, Polticelli F, Bertalan I, Antonacci A, Pastorelli S, Damasso M, Johanningmeier U, Giardi MT. PLoS One 6 e16216 (2011)


Reviews citing this publication (2)

  1. Structure-function investigations of bacterial photosynthetic reaction centers. Leonova MM, Fufina TY, Vasilieva LG, Shuvalov VA. Biochemistry (Mosc) 76 1465-1483 (2011)
  2. Solid-state NMR of nanomachines involved in photosynthetic energy conversion. Alia A, Buda F, de Groot HJ, Matysik J. Annu Rev Biophys 42 675-699 (2013)

Articles citing this publication (16)

  1. Both electronic and vibrational coherences are involved in primary electron transfer in bacterial reaction center. Ma F, Romero E, Jones MR, Novoderezhkin VI, van Grondelle R. Nat Commun 10 933 (2019)
  2. Weak temperature dependence of P (+) H A (-) recombination in mutant Rhodobacter sphaeroides reaction centers. Gibasiewicz K, Białek R, Pajzderska M, Karolczak J, Burdziński G, Jones MR, Brettel K. Photosynth Res 128 243-258 (2016)
  3. 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. Fufina TY, Vasilieva LG, Shuvalov VA. Biochemistry (Mosc) 75 208-213 (2010)
  4. Lipid binding to the carotenoid binding site in photosynthetic reaction centers. Deshmukh SS, Tang K, Kálmán L. J Am Chem Soc 133 16309-16316 (2011)
  5. X-ray structure of the Rhodobacter sphaeroides reaction center with an M197 Phe→His substitution clarifies the properties of the mutant complex. Selikhanov G, Fufina T, Guenther S, Meents A, Gabdulkhakov A, Vasilieva L. IUCrJ 9 261-271 (2022)
  6. Acetyl group orientation modulates the electronic ground-state asymmetry of the special pair in purple bacterial reaction centers. Wawrzyniak PK, Beerepoot MT, de Groot HJ, Buda F. Phys Chem Chem Phys 13 10270-10279 (2011)
  7. Properties of mutant reaction centers of Rhodobacter sphaeroides with substitutions of histidine L153, the axial Mg2+ ligand of bacteriochlorophyll B(A). Leonova MM, Vasilieva LG, Khatypov RA, Boichenko VA, Shuvalov VA. Biochemistry (Mosc) 74 452-460 (2009)
  8. 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)
  9. An investigation of slow charge separation in a tyrosine M210 to tryptophan mutant of the Rhodobacter sphaeroides reaction center by femtosecond mid-infrared spectroscopy. Pawlowicz NP, van Stokkum IH, Breton J, van Grondelle R, Jones MR. Phys Chem Chem Phys 12 2693-2705 (2010)
  10. 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)
  11. 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)
  12. Mutation H(M202)L does not lead to the formation of a heterodimer of the primary electron donor in reaction centers of Rhodobacter sphaeroides when combined with mutation I(M206)H. Khristin AM, Zabelin AA, Fufina TY, Khatypov RA, Proskuryakov II, Shuvalov VA, Shkuropatov AY, Vasilieva LG. Photosynth Res 146 109-121 (2020)
  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. Different effects of identical symmetry-related mutations near the bacteriochlorophyll dimer in the photosynthetic reaction center of Rhodobacter sphaeroides. Vasilieva LG, Fufina TY, Gabdulkhakov AG, Shuvalov VA. Biochemistry (Mosc) 80 647-653 (2015)
  15. Dynamics of diverse coherences in primary charge separation of bacterial reaction center at 77 K revealed by wavelet analysis. Ma F, Romero E, Jones MR, Novoderezhkin VI, Yu LJ, van Grondelle R. Photosynth Res 151 225-234 (2022)
  16. Use of a system of differential equations to analyze the functioning of a catalytic bio macromolecule under non equilibrium conditions. Barabash YM, Serdenko TV, Knox PP, Golub AA. Heliyon 5 e02108 (2019)


Related citations provided by authors (1)

  1. 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)

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