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Title: Reconstitution of the heliobacterial photochemical reaction center and cytochrome c553 into a proteoliposome system

Abstract

The heliobacterial reaction center (HbRC) is the simplest known photochemical reaction center, in terms of its polypeptide composition. In the heliobacterial cells its electron donor is a cytochrome (cyt) c553 attached to the membrane via a covalent linkage with a diacylglycerol. We have reconstituted purified HbRC into liposomes mimicking the phospholipid composition of heliobacterial membranes. We also incorporated a lipid with a headgroup containing Ni(II):nitrilotriacetate (NTA) to provide a binding site for the soluble version of the heliobacterial cyt c553 in which the N-terminal membrane attachment site is replaced by a hexahistidine tag. The HbRC was inserted into the liposomes with the donor side preferentially exposed to the exterior; this bias increased to nearly 100% with higher concentrations (≥10 mole %) of the Ni(II)-NTA lipid in the membrane, and is most likely due to the net negative charge of the surface of the membrane. The HbRC in proteoliposomes without the Ni(II)-NTA lipid exhibited normal charge separation and subsequent charge recombination of the P800+FX- state in 15 ms; however, the oxidized primary donor (P800+) was not significantly reduced by added H6-cyt c553. In contrast, with proteoliposomes containing the Ni(II)-NTA lipid, addition of H6-cyt c553 resulted in a new kinetic component resultingmore » from fast reduction (2-5 ms) of P800+ by H6-cyt c553. The contribution of this kinetic component varied with the concentration of added H6-cyt c553 and could represent 80% or more of the total P800+ decay. Thus, the HbRC and its interaction with its native electron donor have been reconstituted into an artificial membrane system.« less

Authors:
 [1]; ORCiD logo [1]
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  1. Arizona State Univ., Tempe, AZ (United States)
Publication Date:
Research Org.:
Arizona State Univ., Tempe, AZ (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences & Biosciences Division
OSTI Identifier:
1631823
Alternate Identifier(s):
OSTI ID: 1786359; OSTI ID: 1841959
Grant/Contract Number:  
SC0010575
Resource Type:
Accepted Manuscript
Journal Name:
Photosynthesis Research
Additional Journal Information:
Journal Volume: 143; Journal Issue: 3; Journal ID: ISSN 0166-8595
Publisher:
Springer
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; Reaction center; Cytochrome c; Heliobacteria; Proteoliposomes; Reconstitution; reaction center; cytochrome c; heliobacteria; proteoliposomes; reconstitution

Citation Formats

Johnson, William A., and Redding, Kevin E. Reconstitution of the heliobacterial photochemical reaction center and cytochrome c553 into a proteoliposome system. United States: N. p., 2019. Web. doi:10.1007/s11120-019-00695-w.
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Johnson, William A., & Redding, Kevin E. Reconstitution of the heliobacterial photochemical reaction center and cytochrome c553 into a proteoliposome system. United States. https://doi.org/10.1007/s11120-019-00695-w
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Johnson, William A., and Redding, Kevin E. Sat . "Reconstitution of the heliobacterial photochemical reaction center and cytochrome c553 into a proteoliposome system". United States. https://doi.org/10.1007/s11120-019-00695-w. https://www.osti.gov/servlets/purl/1631823.
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@article{osti_1631823,
title = {Reconstitution of the heliobacterial photochemical reaction center and cytochrome c553 into a proteoliposome system},
author = {Johnson, William A. and Redding, Kevin E.},
abstractNote = {The heliobacterial reaction center (HbRC) is the simplest known photochemical reaction center, in terms of its polypeptide composition. In the heliobacterial cells its electron donor is a cytochrome (cyt) c553 attached to the membrane via a covalent linkage with a diacylglycerol. We have reconstituted purified HbRC into liposomes mimicking the phospholipid composition of heliobacterial membranes. We also incorporated a lipid with a headgroup containing Ni(II):nitrilotriacetate (NTA) to provide a binding site for the soluble version of the heliobacterial cyt c553 in which the N-terminal membrane attachment site is replaced by a hexahistidine tag. The HbRC was inserted into the liposomes with the donor side preferentially exposed to the exterior; this bias increased to nearly 100% with higher concentrations (≥10 mole %) of the Ni(II)-NTA lipid in the membrane, and is most likely due to the net negative charge of the surface of the membrane. The HbRC in proteoliposomes without the Ni(II)-NTA lipid exhibited normal charge separation and subsequent charge recombination of the P800+FX- state in 15 ms; however, the oxidized primary donor (P800+) was not significantly reduced by added H6-cyt c553. In contrast, with proteoliposomes containing the Ni(II)-NTA lipid, addition of H6-cyt c553 resulted in a new kinetic component resulting from fast reduction (2-5 ms) of P800+ by H6-cyt c553. The contribution of this kinetic component varied with the concentration of added H6-cyt c553 and could represent 80% or more of the total P800+ decay. Thus, the HbRC and its interaction with its native electron donor have been reconstituted into an artificial membrane system.},
doi = {10.1007/s11120-019-00695-w},
journal = {Photosynthesis Research},
number = 3,
volume = 143,
place = {United States},
year = {Sat Dec 14 00:00:00 EST 2019},
month = {Sat Dec 14 00:00:00 EST 2019}
}
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https://doi.org/10.1007/s11120-019-00695-w
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