Summary
Reaction centers from purple bacteria form a superb test system for the manipulation of electron transfer parameters. The wealth of cofactors and electron transfer reactions provides opportunities for directed modification of specific properties. In particular, the energies of each cofactor can be selectively changed by mutations of neighboring amino acid residues. The starting point for the initial electron transfer, the bacteriochlorophyll dimer, has proven to be exceptionally malleable, allowing large changes in energetics and rates. Most of the other cofactors can be exchanged or eliminated entirely, permitting considerable alteration of pathways. By orchestrating multiple changes in the reaction center, the light-initiated electron transfer pathway can be directed towards alternate ends, for example down the B branch of cofactors rather than the naturally preferred A branch. Extensive modeling of features of electron transfer such as the energetics, the coupling, and the protein dynamics has been corroborated by observed changes in the characteristics of the reactions after modification of the cofactor properties. For example, the maximum rates for several electron transfer reactions, determined by application of Marcus theory to the rates of reactions in a range of mutants, show a correlation with the distance between the cofactors. Other measurements revealing the intimate interaction of the protein and cofactors show that protein motion controls the rate of the initial electron transfer. Thus the reaction center provides a natural and modifiable template for understanding the factors governing electron transfer.
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Keywords
- Electron Transfer
- Reaction Center
- Rhodobacter Sphaeroides
- Free Energy Difference
- Photosynthetic Reaction Center
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
Abbreviations
- BA :
-
bacteriochlorophyll monomer on A branch of cofactors
- BB :
-
bacteriochlorophyll monomer on B branch of cofactors
- HA :
-
bacteriopheophytin on A branch of cofactors
- HB :
-
bacteriopheophytin on B branch of cofactors
- P:
-
bacteriochlorophyll dimer
- QA :
-
quinone on A branch of cofactors
- QB :
-
quinone on B branch of cofactors
- Rba. :
-
Rhodobacter
References
Alden RG, Parson WW, Chu ZT and Warshel A (1996) Orientation of the OH dipole of tyrosine (M)210 and its effect on electrostatic energies in photosynthetic bacterial reaction centers. J Phys Chem 100: 16761–16770
Allen JP and Williams JC (1995) Relationship between the oxidation potential of the bacteriochlorophyll dimer and electron transfer in photosynthetic reaction centers. J Bioenerg Biomembr 27: 275–283
Allen JP and Williams JC (2006) The influence of protein interactions on the properties of the bacteriochlorophyll dimer in reaction centers. In: Grimm B, Porra RJ, Rüdiger W and Scheer H (eds) Chlorophylls and Bacteriochlorophylls: Biochemistry, Biophysics, Functions and Applications (Advances in Photosynthesis and Respiration, Vol 25), pp 283–295. Springer, Dordrecht
Allen JP, Artz K, Lin X, Williams JC, Ivancich A, Albouy D, Mattioli TA, Fetsch A, Kuhn M and Lubitz W (1996) Effects of hydrogen bonding to abacteriochlorophyll-bacteriopheophytin dimer in reaction centers from Rhodobacter sphaeroides. Biochemistry 35: 6612–6619
Allen JP, Williams JC, Graige MS, Paddock ML, Labahn A, Feher G and Okamura MY (1998) Free energy dependence of the direct charge recombination from the primary and secondary quinones in reaction centers from Rhodobacter sphaeroides. Photosynth Res 55: 227–233
Arlt T, Dohse B, Schmidt S, Wachtveitl J, Laussermair E, Zinth W and Oesterhelt D (1996) Electron transfer dynamics of Rhodopseudomonas viridis reaction centers with a modified binding site forthe accessory bacteriochlorophyll. Biochemistry 35: 9235–9244
Artz K, Williams JC, Allen JP, Lendzian F, Rautter J and Lubitz W (1997) Relationship between the oxidation potential and electron spin density of the primary electron donor in reaction centers from Rhodobacter sphaeroides. Proc Natl Acad Sci USA 94: 13582–13587
Breton J, Wakeham MC, Fyfe PK, Jones MR and Nabedryk E (2004) Characterization of the bonding interactions of QB upon photoreduction via A-branch or B-branch electron transfer in mutant reaction centers from Rhodobacter sphaeroides. Biochim Biophys Acta 1656: 127–138
Bylina EJ and Youvan DC (1988) Directed mutations affecting spectroscopic and electron transfer properties of the primary donor in the photosynthetic reaction center. Proc Natl Acad Sci USA 85: 7226–7230
Bylina EJ, Kirmaier C, McDowell L, Holten D and Youvan DC (1988) Influence of an amino-acid residue on the optical properties and electron transfer dynamics of a photosynthetic reaction centre complex. Nature 336: 182–184
Bylina EJ, Kolaczkowski SV, Norris JR and Youvan DC (1990) EPR characterization of genetically modified reaction centers of Rhodobacter capsulatus. Biochemistry 29: 6203–6210
Chen L, Holten D, Bocian DF and Kirmaier C (2004) Effects of hydrogen bonding and structure of the accessory bacteriochlorophylls on charge separation in Rb. capsulatus reaction centers. J Phys Chem B 108: 10457–10464
Chuang JI, Boxer SG, Holten D and Kirmaier C (2006) High yield of M-side electron transfer in mutants of Rhodobacter capsulatus reaction centers lacking the L-side bacteriopheophytin. Biochemistry 45: 3845–3851
Dahlbom MG and Reimers JR (2005) Successes and failures of time-dependent density functional theory for the low-lying excited states of chlorophylls. Mol Phys 103: 1057–1065
de Boer AL, Neerken S, de Wijn R, Permentier HP, Gast P, Vijgenboom E and Hoff AJ (2002) B-branch electron transfer in reaction centers of Rhodobacter sphaeroides assessed with site-directed mutagenesis. Photosynth Res 71: 221–239
Finkele U, Lauterwasser C, Zinth W, Gray KA and Oesterhelt D (1990) Role of tyrosine M210 in the initial charge separation of reaction centers of Rhodobacter sphaeroides. Biochemistry 29: 8517–8521
Frolov D, Wakeham MC, Andrizhiyevskaya EG, Jones MR and van Grondelle R (2005) Investigation of B-branch electron transfer by femtosecond time resolved spectroscopy in a Rhodobacter sphaeroides reaction centre that lacks the QA ubiquinone. Biochim Biophys Acta 1707: 189–198
Gehlen JN, Marchi M and Chandler D (1994) Dynamics affecting the primary charge transfer in photosynthesis. Science 263: 499–502
Goldsmith JO, King B and Boxer SG (1996) Mg coordination by amino acid side chains is not required for assembly and function of the special pair in bacterial photosynthetic reaction centers. Biochemistry 35: 2421–2428
Gray HB and Winkler JR (2005) Long-range electron transfer. Proc Natl Acad Sci USA 102: 3534–3539
Gunner MR, Nicholls A and Honig B (1996) Electrostatic potentials in Rhodopseudomonas viridis reaction centers: Implications for the driving force and directionality of electron transfer. J Phys Chem 100: 4277–4291
Haffa ALM, Lin S, Katilius E, Williams JC, Taguchi AKW, Allen JP and Woodbury NW (2002) The dependence of the initial electron-transfer rate on driving force in Rhodobacter sphaeroides reaction centers. J Phys Chem 106: 7376–7384
Haffa ALM, Lin S, Williams JC, Taguchi AKW, Allen JP and Woodbury NW (2003) High yield of long-lived B-side charge separation at room temperature in mutant bacterial reaction centers. J Phys Chem B 107: 12503–12510
Haffa ALM, Lin S, Williams JC, Bowen BP, Taguchi AKW, Allen JP and Woodbury NW (2004) Controlling the pathway of photosynthetic charge separation in bacterial reaction centers. J Phys Chem B 108: 4–7
Heller BA, Holten D and Kirmaier C (1995) Control of electron transfer between the L- and M-sides of photosynthetic reaction centers. Science 269: 940–945
Ishikita H, Loll B, Biesiadka J, Galstyan A, Saenger W and Knapp EW (2005) Tuning electron transfer by ester-group of chlorophylls in bacterial photosynthetic reaction center. FEBS Lett 579: 712–716
Ishikita H, Saenger W, Loll B, Biesiadka J and Knapp EW (2006) Energetics of a possible proton exit pathway for water oxidation in Photosystem II. Biochemistry 45: 2063–2071
Jackson JA, Lin S, Taguchi AKW, Williams JC, Allen JP and Woodbury NW (1997) Energy transfer in Rhodobacter sphaeroides reaction centers with the initial electron donor oxidized or missing. J Phys Chem B 101: 5747–5754
Jia Y, DiMagno TJ, Chan CK, Wang Z, Du M, Hanson DK, Schiffer M, Norris JR, Fleming GR and Popov MS (1993) Primary charge separation in mutant reaction centers of Rhodobacter capsulatus. J Phys Chem 97: 13180–13191
Johnson ET and Parson WW (2002) Electrostatic interactions in an integral membrane protein. Biochemistry 41: 6483–6494
Johnson ET, Müh F, Nabedryk E, Williams JC, Allen JP, Lubitz W, Breton J and Parson WW (2002) Electronic and vibronic coupling of the special pair of bacteriochlorophylls in photosynthetic reaction centers from wild-type and mutant strains of Rhodobacter sphaeroides. J Phys Chem B 106: 11859–11869
Kálmán L, LoBrutto R, Allen JP and Williams JC (1999) Modified reaction centres oxidize tyrosine in reactions that mirror Photosystem II. Nature 402: 696–699
Kálmán L, Williams JC and Allen JP (2003a) Proton release upon oxidation of tyrosine in reaction centers from Rhodobacter sphaeroides. FEBS Lett 545: 193–198
Kálmán L, LoBrutto R, Narváez AJ, Williams JC and Allen JP (2003b) Correlation of proton release and electrochromic shifts of the optical spectrum due to oxidation of tyrosine in reaction centers from Rhodobacter sphaeroides. Biochemistry 42: 13280–13286
Kálmán L, Thielges MC, Williams JC and Allen JP (2005) Proton release due to manganese binding and oxidation in modified bacterial reaction centers. Biochemistry 44: 13266–13273
Kanchanawong P, Dahlbom MG, Treynor TP, Reimers JR, Hush NS and Boxer SG (2006) Charge delocalization in the specialpair radical cation of mutant reaction centers of Rhodobacter sphaeroides from Stark spectra and nonadiabatic spectral simulations. J Phys Chem B 110: 18688–18702
Katilius E, Turanchik T, Lin S, Taguchi AKW and Woodbury NW (1999) B-side electron transfer in a Rhodobacter sphaeroides reaction center mutant in which the B-side monomer bacteriochlorophyll is replaced with bacteriopheophytin. J Phys Chem B 103: 7386–7389
Katilius E, Katiliene Z, Lin S, Taguchi AKW and Woodbury NW (2002a) B side electron transfer in a Rhodobacter sphaeroides reaction center mutant in which the B side monomer bacteriochlorophyll is replaced with bacteriopheophytin: Low-temperature study and energetics of charge-separated states. J Phys Chem B 106: 1471–1475
Katilius E, Katiliene Z, Lin S, Taguchi AKW and Woodbury NW (2002b) B-side electron transfer in the HE(M182) reaction center mutant from Rhodobacter sphaeroides. J Phys Chem B 106: 12344–12350
Katilius E, Babendure JL, Katiliene Z, Lin S, Taguchi AKW and Woodbury NW (2003) Manipulations of the B-side chargeseparated states’ energetics in the Rhodobacter sphaeroides reaction center. J Phys Chem B 107: 12029–12034
Katilius E, Babendure JL, Lin S and Woodbury NW (2004) Electron transfer dynamics in Rhodobacter sphaeroides reaction center mutants with a modified ligand for the monomer bacteriochlorophyll on the active side. Photosynth Res 81: 165–180
Kee HL, Laible PD, Bautista JA, Hanson DK, Holten D and Kirmaier C (2006) Determination of the rate and yield of B-side quinone reduction in Rhodobacter capsulatus reaction centers. Biochemistry 45: 7314–7322
Khatypov RA, Vasilieva LG, Fufina TY, Bolgarina TI and Shuvalov VA (2005) Substitution of isoleucine L177 by histidine affects the pigment composition and properties of the reaction center of the purple bacterium Rhodobacter sphaeroides. Biochemistry (Moscow) 70: 1527–1533
King BA, de Winter A, McAnaney TB and Boxer SG (2001) Excited state energy transfer pathways in photosynthetic reaction centers. 4. Asymmetric energy transfer in the heterodimer mutant. J Phys Chem B 105: 1856–1862
Kirmaier C, Holten, D, Bylina EJ and Youvan DC (1988) Electron transfer in a genetically modified bacterial reaction center containing a heterodimer. Proc Natl Acad Sci USA 85: 7562–7566
Kirmaier C, Gaul D, DeBey R, Holten D and Schenck CC (1991) Charge separation in a reaction center incorporating bacteriochlorophyll for photoactive bacteriopheophytin. Science 251: 922–927
Kirmaier C, Weems D and Holten D (1999) M-side electron transfer in reaction center mutants with a lysine near the nonphotoactive bacteriochlorophyll. Biochemistry 38: 11516–11530
Kirmaier C, He C and Holten D (2001) Manipulating the direction of electron transfer in the bacterial reaction center by swapping Phe for Tyr near BChlM (L181) and Tyr for Phe near BChlL (M208). Biochemistry 40: 12132–12139
Kirmaier C, Cua A, He C, Holten D and Bocian DF (2002a) Probing the M-branch electron transfer and cofactor environment in the bacterial photosynthetic reaction center by addition of a hydrogen bond to the M-side bacteriopheophytin. J Phys Chem B 106: 495–503
Kirmaier C, Laible PD, Czarnecki K, Hata AN, Hanson DK, Bocian DF and Holten D (2002b) Comparison of M-side electron transfer in Rb. sphaeroides and Rb. capsulatus reaction centers. J Phys Chem B 106: 1799–1808
Kirmaier C, Laible PD, Hanson DK and Holten D (2003) B-side charge separation in bacterial photosynthetic reaction centers: nanosecond time scale electron transfer from HB - to QB. Biochemistry 42: 2016–2024
Kirmaier C, Laible PD, Hanson DK and Holten D (2004) B-side electron transfer to form P+HB - in reaction centers from the F(L181)Y/Y(M208)F mutant of Rhodobacter capsulatus. J Phys Chem B 108: 11827–11832
Kirmaier C, Bautista JA, Laible PD, Hanson DK and Holten D (2005) Probing the contribution of electronic coupling to the directionality of electron transfer in photosynthetic reaction centers. J Phys Chem B 109: 24160–24172
Laible PD, Kirmaier C, Udawatte CSM, Hofman SJ, Holten D and Hanson DK (2003) Quinone reduction via secondary B-branch electron transfer in mutant bacterial reaction centers. Biochemistry 42: 1718–1730
Li Y, Lucas MG, Konovalova T, Abbott B, MacMillan F, Petrenko A, Sivakumar V, Wang R, Hastings G, Gu F, van Tol J, Brunei LC, Timkovich R, Rappaport F and Redding K (2004) Mutation of the putative hydrogen-bond donor to P700 of Photosystem I. Biochemistry 43: 12634–12647
Li Y, van der Est A, Lucas MG, Ramesh VM, Gu F, Petrenko A, Lin S, Webber AN, Rappaport F and Redding K (2006) Directing electron transfer within Photosystem I by breaking H-bonds in the cofactor branches. Proc Natl Acad Sci USA 103: 2144–2149
Lin J and Beratan DN (2005) Simulation of electron transfer between cytochrome c 2 and the bacterial photosynthetic reaction center: Brownian dynamics analysis of the native proteins and double mutants. J Phys Chem B 109: 7529–7534
Lin J, Balabin IA and Beratan DN (2005) The nature of aqueous tunneling pathways between electron-transferproteins. Science 310: 1311–1313
Lin S, Katilius E, Haifa ALM, Taguchi AKW and Woodbury NW (2001) Blue light drives B-side electron transfer in bacterial photosynthetic reaction centers. Biochemistry 40: 13767–13773
Lin S, Katilius E, Taguchi AKW and Woodbury NW (2003) Excitation energy transfer from carotenoid to bacteriochlorophyll in the photosynthetic purple bacterial reaction center of Rhodobacter sphaeroides. J Phys Chem B 107: 14103–14108
Lin X, Murchison HA, Nagarajan V, Parson WW, Allen JP and Williams JC (1994a) Specific alteration of the oxidation potential of the electron donor in reaction centers from Rhodobacter sphaeroides. Proc Natl Acad Sci USA 91: 10265–10269
Lin X, Williams JC, Allen JP and Mathis P (1994b) Relationship between rate and free energy difference for electron transfer from cytochrome c 2 to the reaction center in Rhodobacter sphaeroides. Biochemistry 33: 13517–13523
Marcus RA and Sutin N (1985) Electron transfers in chemistry and biology. Biochim Biophys Acta 811: 265–322
McDowell LM, Gaul D, Kirmaier C, Holten D and Schenck CC (1991) Investigation into the source of electron transfer asymmetry in bacterial reaction centers. Biochemistry 30: 8315–8322
Middendorf TR, Mazzola LT, Lao K, Steffen MA and Boxer SG (1993) Stark effect (electroabsorption) spectroscopy of photosynthetic reaction centers at 1.5 K: Evidence that the special pair has a large excited-state polarizability. Biochim Biophys Acta 1143: 223–234
Miyashita O, Okamura MY and Onuchic JN (2005) Interprotein electron transfer from cytochrome c 2 to photosynthetic reaction center: Tunneling across an aqueous interface. Proc Natl Acad Sci USA 102: 3558–3563
Moore LJ and Boxer SG (1998) Inter-chromophore interactions in pigment-modified and dimer-less bacterial photosynthetic reaction centers. Photosynth Res 55: 173–180
Müh F, Williams, JC, Allen JP and Lubitz W (1998) A conformational change of the photoactive bacteriopheophytin in reaction centers from Rhodobacter sphaeroides. Biochemistry 37: 13066–13074
Müh F, Lendzian F, Roy M, Williams JC, Allen JP and Lubitz W (2002) Pigment-protein interactions in bacterial reaction centers and their influence on oxidation potential and spin density distribution of the primary donor. J Phys Chem B 106: 3226–3236
Murchison HA, Alden RG, Allen JP, Peloquin JM, Taguchi AKW, Woodbury NW and Williams JC (1993) Mutations designed to modify the environment of the primary electron donor of the reaction center from Rhodobacter sphaeroides: Phenylalanine to leucine at L167 and histidine to phenylalanine at L168. Biochemistry 32: 3498–3505
Nagarajan V, Parson WW, Gaul D and Schenck C (1990) Effect of specific mutations of tyrosine-(M)210 on the primary photosynthetic electron-transferprocess in Rhodobacter sphaeroides. Proc Natl Acad Sci USA 87: 7888–7892
Narváez AJ, Kálmán L, LoBrutto R, Allen JP and Williams JC (2002) Influence of the protein environment on the properties of a tyrosyl radical in reaction centers from Rhodobacter sphaeroides. Biochemistry 41: 15253–15258
Narváez AJ, LoBrutto R, Allen JP and Williams JC (2004) Trapped tyrosyl radical populations in modified reaction centers from Rhodobacter sphaeroides. Biochemistry 43: 14379–14384
Noy D, Moser CC and Dutton PL (2006) Design and engineering of photosynthetic light-harvesting and electron transfer using length, time, and energy scales. Biochim Biophys Acta 1757: 90–105
Paddock ML, Chang C, Xu Q, Abresch EC, Axelrod HL, Feher G and Okamura MY (2005) Quinone (QB) reduction by B-branch electron transfer in mutant bacterial reaction centers from Rhodobacter sphaeroides: quantum efficiency and X-ray structure. Biochemistry 44: 6920–6928
Paddock ML, Flores M, Isaacson R, Chang C, Abresch EC, Selvaduray P and Okamura MY (2006) Trapped conformational states of semiquinone (D+•QB -•) formed by B-branch electron transfer at low temperature in Rhodobacter sphaeroides reaction centers. Biochemistry 45: 14032–14042
Parson WW, Chu ZT and Warshel A (1990) Electrostatic control of charge separation in bacterial photosynthesis. Biochim Biophys Acta 1017: 251–272
Plato M, Lendzian F, Lubitz W and Möbius K (1992) Molecular orbital study of electronic asymmetry in primary donors of bacterial reaction centers. In: Breton J and Verméglio A (eds) The Photosynthetic Bacterial Reaction Center II: Structure, Spectroscopy, and Dynamics, pp 109–118. Plenum, New York
Potter JA, Fyfe PK, Frolov D, Wakeham MC, van Grondelle R, Robert B and Jones MR (2005) Strong effects of an individual water molecule on the rate of light-driven charge separation in the Rhodobacter sphaeroides reaction center. J Biol Chem 280: 27155–27164
Reimers JR and Hush NS (2004) A unified description of the electrochemical, charge distribution, and spectroscopic properties of the special-pair radical cation in bacterial photosynthesis. J Am Chem Soc 126: 4132–4144
Robles SJ, Breton J and Youvan DC (1990) Partial symmetrization of the photosynthetic reaction center. Science 248: 1402–1405
Spiedel D, Jones MR and Robert B (2002) Tuning of the redox potential of the primary electron donor in reaction centres of purple bacteria: Effects of amino acid polarity and position. FEBS Lett 527: 171–175
Stocker JW, Taguchi AKW, Murchison HA, Woodbury NW and Boxer SG (1992) Spectroscopic and redox properties of sym1 and (M)F 195H: Rhodobacter capsulatus reaction center symmetry mutants which affect the initial electron donor. Biochemistry 31: 10356–10362
Sumi H and Marcus RA (1986) Dielectric relaxation and intramolecular electron transfers. J Chem Phys 84: 4272–4276
Thielges M, Uyeda G, Cámara-Artigas A, Kálmán L, Williams JC and Allen JP (2005) Design of a redox-linked active metal site: Manganese bound to bacterial reaction centers at a site resembling that of Photosystem II. Biochemistry 44: 7389–7394
Treynor TP, Yoshina-Ishii C and Boxer SG (2004) Probing excited-state electron transfer by resonance Stark spectroscopy: 4. Mutations near BL in photosynthetic reaction centers perturb multiple factors that affect BL* → BL +HL -. J Phys Chem B 108: 13523–13535
van Brederode ME, van Stokkum IHM, Katilius E, van Mourik F, Jones MR and van Grondelle R (1999) Primary charge separation routes in the BChl:Bphe heterodimer reaction centers of Rhodobacter sphaeroides. Biochemistry 38: 7545–7555
Wakeham MC and Jones MR (2005) Rewiring photosynthesis: Engineering wrong-way electron transfer in the purple bacterial reaction centre. Biochem Soc Trans 33: 851–857
Wakeham MC, Goodwin MG, McKibbin C and Jones MR (2003) Photo-accumulation of the P+QB - radical pair state in purple bacterial reaction centres that lack the QA ubiquinone. FEBS Lett 540: 234–240
Wakeham MC, Breton J, Nabedryk E and Jones MR (2004) Formation of a semiquinone at the QB site by A- or B-branch electron transfer in the reaction center from Rhodobacter sphaeroides. Biochemistry 43: 4755–4763
Wang H, Lin S and Woodbury NW (2006) Electronic transitions of the Soret band of reaction centers from Rhodobacter sphaeroides studied by femtosecond transient absorbance spectroscopy. J Phys Chem B 110: 6956–6961
Wang H, Lin S, Allen JP, Williams JC, Blankert S, Laser C and Woodbury NW (2007) Protein dynamics control the kinetics of initial electron transfer in photosynthesis. Science 316: 747–750
Warshel A, Chu ZT and Parson WW (1989) Dispersed polaron simulations of electron transfer in photosynthetic reaction centers. Science 246: 112–116
Watson AJ, Fyfe PK, Frolov D, Wakeham MC, Nabedryk E, van Grondelle R, Breton J and Jones MR (2005) Replacement or exclusion of the B-branch bacteriopheophytin in the purple bacterial reaction centre: The HB cofactor is not required for assembly or core function of the Rhodobacter sphaeroides complex. Biochim Biophys Acta 1710: 34–46
Webber AN and Lubitz W (2001) P700: The primary electron donor of Photosystem I. Biochim Biophys Acta 1507: 61–79
Williams JC, Alden RG, Murchison HA, Peloquin JM, Woodbury NW and Allen JP (1992) Effects of mutations near the bacteriochlorophylls in reaction centers from Rhodobacter sphaeroides. Biochemistry 31: 11029–11037
Williams JC, Haffa ALM, McCulley JL, Woodbury NW and Allen JP (2001) Electrostatic interactions between charged amino acid residues and the bacteriochlorophyll dimer in reaction centers from Rhodobacter sphaeroides. Biochemistry 40: 15403–15407
Williams JC, Paddock ML, Way YP and Allen JP (2007) Changes in metal specificity due to iron ligand substitutions in reaction centers from Rhodobacter sphaeroides. Appl Magn Reson 31: 45–58
Witt H, Schlodder E, Teutloff C, Niklas J, Bordignon E, Carbonera D, Kohler S, Labahn A and Lubitz W (2002) Hydrogen bonding to P700: site-directed mutagenesis of threonine A739 of Photosystem I in Chlamydomonas reinhardtii. Biochemistry 41: 8557–8569
Yakovlev AG, Jones MR, Potter JA, Fyfe PK, Vasilieva LG, Shkuropatov AY and Shuvalov VA (2005) Primary charge separation between P* and BA: Electron-transfer pathways in native and mutant GM203L bacterial reaction centers. Chem Phys 319: 297–307
Yanagi K, Shimizu M, Hashimoto H, Gardiner AT, Roszak AW and Cogdell RJ (2005) Local electrostatic field induced by the carotenoid bound to the reaction center of the purple photosynthetic bacterium Rhodobacter sphaeroides. J Phys Chem B 109: 992–998
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Williams, J.C., Allen, J.P. (2009). Directed Modification of Reaction Centers from Purple Bacteria. In: Hunter, C.N., Daldal, F., Thurnauer, M.C., Beatty, J.T. (eds) The Purple Phototrophic Bacteria. Advances in Photosynthesis and Respiration, vol 28. Springer, Dordrecht. https://doi.org/10.1007/978-1-4020-8815-5_18
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