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Structural Plasticity of Reaction Centers from Purple Bacteria

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The Purple Phototrophic Bacteria

Part of the book series: Advances in Photosynthesis and Respiration ((AIPH,volume 28))

Summary

The purple bacterial reaction center has made major contributions to our understanding of photosynthetic energy transduction and biological electron transfer. A major element in this work has been alteration of the structure and/or composition of the reaction center through site-directed mutagenesis or biochemical treatments, and much of the usefulness of the reaction center as an experimental system has come from its (sometimes surprising) tolerance of significant changes in cofactor composition or amino acid sequence. The purpose of this chapter is to illustrate this structural plasticity, by documenting the extent to which the structure and composition of the reaction center has been altered in order to investigate details of its mechanism, or general principles pertaining to biological electron transfer. For the cofactors, the article looks at how and why individual cofactors have been replaced and the main outcomes of such studies. For the protein, the emphasis is placed on mutations involving large numbers of amino acids or single mutations that alter the cofactor composition of the complex. The chapter also considers the significant influence that changes in solvent (water) structure can have on reaction center structure and mechanism, attempts to construct chimeric reaction centers, and protein engineering aimed at introducing new functionality into the reaction center.

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Abbreviations

BA :

A-side monomeric BChl

BB :

B-side monomeric BChl

BChl:

bacteriochlorophyll

Blc. :

Blastochloris

BPhe:

bacteriopheophytin

Chl:

chlorophyll

EmP/P+ :

mid-point redox potential of P/P+

HA :

A-side BPhe

HB :

B-side BPhe

LDAO:

lauryldimethylamine oxide

LH1:

core light harvesting complex

LH2:

peripheral light harvesting complex

P:

primary electron donor

PA :

A-side P BChl

PB :

B-side P BChl

QA :

primary acceptor quinone

QB :

secondary (dissociable) acceptor quinone

Rba. :

Rhodobacter

RC:

reaction center

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Authors and Affiliations

  1. Department of Biochemistry, School of Medical Sciences, University of Bristol, University Walk, Bristol, BS8 1TD, UK

    Michael R. Jones

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  1. Michael R. Jones
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Correspondence to Michael R. Jones .

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Editors and Affiliations

  1. University of Sheffield, UK

    C. Neil Hunter

  2. University of Pennsylvania, USA

    Fevzi Daldal

  3. Argonne National Laboratory, USA

    Marion C. Thurnauer

  4. University of British Columbia, Canada

    J. Thomas Beatty

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© 2009 Springer Science + Business Media B.V

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Jones, M.R. (2009). Structural Plasticity 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_16

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