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Structure-Function Relationships in Bacterial Light-Harvesting Complexes Investigated by Reconstitution Techniques

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The Purple Phototrophic Bacteria

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

Summary

Exploration of conditions to achieve the reversible dissociation of the core light-harvesting complexes (LH1) of photosynthetic bacteria led to the isolation of the fundamental subunit complex, B820. Further reversible dissociation of B820 provided conditions for reconstitution of both this subunit complex and LH1 from separately isolated polypeptides and bacteriochlorophyll (BChl). Native-like LH1 complexes have also been reconstituted using BChl, isolated polypeptides from Rhodospirillum (Rsp.) rubrum or Rhodobacter (Rba.) sphaeroides and carotenoid. The reconstitution methodology has also been applied to the peripheral light-harvesting complex (LH2) of Phaeospirillum (Phs.) molischianum in which it was demonstrated that LH2 contained the same B820-type subunit structure found in LH1.

Since the interaction between B820 and its individual components could be studied under equilibrium conditions, many structure-function questions could be addressed as well as thermodynamic parameters established. The subunit structure was shown to consist of α1β1·2BChl with overlap at rings III and V of the BChls. Minimal requirements for B820 formation include (1) a polypeptide of at least 26 amino acids, 18 of which constitute an α-helix with hydrophobic side chains, (2) a His residue for coordination and hydrogen bonding to BChl and (3) a Trp residue for hydrogen bonding to the C31 carbonyl of BChl. The His interaction accounted for over half of the stabilization energy of the B820 complex. Hydrogen bonds involving the Trp residues provide a second major stabilization of approximately 3.5 kcal/Trp. Finally, some stabilization is provided by specific interactions between the α and β polypeptides in their N-terminal regions, most likely exhibiting the same structural motif as found in the crystal structure of Phs. molischianum LH2.

Reconstitution methodology has also been used to study formation of the reaction center-LH1 (RC-LH1) core complex, which exhibited physical properties analogous to the native complex, and to study the interaction and function of PufX. Currently, the isolation and reconstitution methodology is being applied to reconstitute the RC from its fundamental components.

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Abbreviations

BChl:

bacteriochlorophyll; BChl a is implied unless BChl b is indicated

CD:

circular dichroism

EM:

electron microscopy

HPLC:

high performance liquid chromatography

K A :

association constant for binding

K D :

dissociation constant for binding

LH1:

core light-harvesting complex, also called B875, B890, etc. depending on the far-red absorption maximum

LH2:

peripheral light-harvesting complex, also called B800-850, for example

NMR:

nuclear magnetic resonance

PAGE:

polyacrylamide gel electrophoresis

Phs. :

Phaeospirillum

PRC:

photoreceptor complex which contains LH1 and RC

QB :

quinone on the B-side of the reaction center

Rba. :

Rhodobacter

RC:

reaction center

Rps. :

Rhodopseudomonas

RR:

resonance Raman

Rsp. :

Rhodospirillum

SDS:

sodium dodecyl sulfate

UQ:

ubiquinone

β-OG:

n-octyl β-D-glucopyranoside

λmax :

wavelength of maximum absorption

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Authors and Affiliations

  1. Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, 2205 Tech Drive, Evanston, IL, 60208-3500, USA

    Paul A. Loach & Pamela S. Parkes-Loach

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  1. Paul A. Loach
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Correspondence to Paul A. Loach .

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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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Loach, P.A., Parkes-Loach, P.S. (2009). Structure-Function Relationships in Bacterial Light-Harvesting Complexes Investigated by Reconstitution Techniques. 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_10

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