A series of reaction centres bearing mutations at the (Phe) M197 position were constructed in the photosynthetic bacterium Rhodobacter sphaeroides. This residue is adjacent to the pair of bacteriochlorophyll molecules (PL and PM) that is the primary donor of electrons (P) in photosynthetic light-energy transduction. All of the mutations affected the optical and electrochemical properties of the P bacteriochlorophylls. A mutant reaction centre with the change Phe M197 to Arg (FM197R) was crystallized, and a structural model constructed at 2.3 Å (1Å = 0.1nm) resolution. The mutation resulted in a change in the structure of the protein at the interface region between the P bacteriochlorophylls and the monomeric bacteriochlorophyll that is the first electron acceptor (BL). The new Arg residue at the M197 position undergoes a significant reorientation, creating a cavity at the interface region between P and BL. The acetyl carbonyl substituent group of the PM bacteriochlorophyll undergoes an out-of-plane rotation, which decreases the edge-to-edge distance between the macrocycles of PM and BL. In addition, two new buried water molecules partially filled the cavity that is created by the reorientation of the Arg residue. These waters are in a suitable position to connect the macrocycles of P and BL via three hydrogen bonds. Transient absorption measurements show that, despite an inferred decrease in the driving force for primary electron transfer in the FM197R reaction centre, there is little effect on the overall rate of the primary reaction in the bulk of the reaction-centre population. Examination of the X-ray crystal structure reveals a number of small changes in the structure of the reaction centre in the interface region between the P and BL bacteriochlorophylls that could account for this faster-than-predicted rate of primary electron transfer.
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November 2000
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Research Article|
October 24 2000
An examination of how structural changes can affect the rate of electron transfer in a mutated bacterial photoreaction centre
Justin P. RIDGE;
Justin P. RIDGE
1
*Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, Sheffield S10 2UH, U.K.
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Paul K. FYFE;
Paul K. FYFE
†Department of Biochemistry, School of Medical Sciences, University of Bristol, University Walk, Bristol BS8 1TD, U.K.
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Katherine E. McAULEY;
Katherine E. McAULEY
2
‡Department of Chemistry, University of Glasgow, Glasgow G12 8QQ, U.K.
§Division of Biochemistry and Molecular Biology, University of Glasgow, Glasgow G12 8QQ, U.K.
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Marion E. VAN BREDERODE;
Marion E. VAN BREDERODE
¶Department of Physics and Astronomy, Free University of Amsterdam, De Boelelaan 1081, HV 1081 Amsterdam, The Netherlands
ǁInterfaculty Reactor Institute, Department of Radiation Chemistry, University of Technology TU Delft, The Netherlands
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Bruno ROBERT;
Bruno ROBERT
**Section de Biophysique des Protéines et des Membranes, DBCM/CEA and URA 1290 CNRS, C. E. Saclay, 91191 Gif/Yvette, France
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Rienk VAN GRONDELLE;
Rienk VAN GRONDELLE
¶Department of Physics and Astronomy, Free University of Amsterdam, De Boelelaan 1081, HV 1081 Amsterdam, The Netherlands
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Neil W. ISAACS;
Neil W. ISAACS
‡Department of Chemistry, University of Glasgow, Glasgow G12 8QQ, U.K.
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Richard J. COGDELL;
Richard J. COGDELL
§Division of Biochemistry and Molecular Biology, University of Glasgow, Glasgow G12 8QQ, U.K.
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Michael R. JONES
Michael R. JONES
3
†Department of Biochemistry, School of Medical Sciences, University of Bristol, University Walk, Bristol BS8 1TD, U.K.
3To whom correspondence should be addressed (e-mail m.r.jones@bristol.ac.uk).
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Publisher: Portland Press Ltd
Received:
June 14 2000
Revision Received:
July 24 2000
Accepted:
August 17 2000
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London © 2000
2000
Biochem J (2000) 351 (3): 567–578.
Article history
Received:
June 14 2000
Revision Received:
July 24 2000
Accepted:
August 17 2000
Citation
Justin P. RIDGE, Paul K. FYFE, Katherine E. McAULEY, Marion E. VAN BREDERODE, Bruno ROBERT, Rienk VAN GRONDELLE, Neil W. ISAACS, Richard J. COGDELL, Michael R. JONES; An examination of how structural changes can affect the rate of electron transfer in a mutated bacterial photoreaction centre. Biochem J 1 November 2000; 351 (3): 567–578. doi: https://doi.org/10.1042/bj3510567
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