Bacterial Light-Harvesting Complexes Showing Giant Second-Order Nonlinear Optical Response as Revealed by Hyper-Rayleigh Light Scattering

Ma, Fang; Yu, Long; Hua, Xiao Ming; Wang, Peng; Wang-Otomo, Zheng-Yu; Zhang, Jian Ping

doi:10.1021/acs.jpcb.6b07461

Cited by 4 publications

(5 citation statements)

References 44 publications

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“…sphaeroides strain DP2 (Figure ). This conclusion is also consistent with the fact that selective removal of the carotenoids from LH1 complexes results in a blue shift of ∼10 nm for the LH1-Q y band. , …”

Section: Resultssupporting

confidence: 88%

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Biochemical and Spectroscopic Characterizations of a Hybrid Light-Harvesting Reaction Center Core Complex

et al. 2018

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The light-harvesting 1 reaction center (LH1-RC) complex from Thermochromatium tepidum exhibits a largely red-shifted LH1 Q absorption at 915 nm due to binding of Ca, resulting in an "uphill" energy transfer from LH1 to the reaction center (RC). In a recent study, we developed a heterologous expression system (strain TS2) to construct a functional hybrid LH1-RC with LH1 from Tch. tepidum and the RC from Rhodobacter sphaeroides [Nagashima, K. V. P., et al. (2017) Proc. Natl. Acad. Sci. U. S. A. 114, 10906]. Here, we present detailed characterizations of the hybrid LH1-RC from strain TS2. Effects of metal cations on the phototrophic growth of strain TS2 revealed that Ca is an indispensable element for its growth, which is also true for Tch. tepidum but not for Rba. sphaeroides. The thermal stability of the TS2 LH1-RC was strongly dependent on Ca in a manner similar to that of the native Tch. tepidum, but interactions between the heterologous LH1 and RC became relatively weaker in strain TS2. A Fourier transform infrared analysis demonstrated that the Ca-binding site of TS2 LH1 was similar but not identical to that of Tch. tepidum. Steady-state and time-resolved fluorescence measurements revealed that the uphill energy transfer rate from LH1 to the RC was related to the energy gap in an order of Rba. sphaeroides, Tch. tepidum, and strain TS2; however, the quantum yields of LH1 fluorescence did not exhibit such a correlation. On the basis of these findings, we discuss the roles of Ca, interactions between LH1 and the RC from different species, and the uphill energy transfer mechanisms.

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Section: Resultssupporting

confidence: 88%

“…This conclusion is also consistent with the fact that selective removal of the carotenoids from LH1 complexes results in a blue shift of ∼10 nm for the LH1-Q y band. 23,24 Uphill Energy Transfer Rate. To determine the uphill energy transfer rates, we measured fluorescence lifetimes of the RC from the Tch.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Biochemical and Spectroscopic Characterizations of a Hybrid Light-Harvesting Reaction Center Core Complex

et al. 2018

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“…The LH1-RC fraction was eluted by a linear gradient of CaCl 2 from 0 mM to 100 mM. The peak fractions with A 877 / A 280 > 2.2 were collected for subsequent measurement (Figure S1a), and then assessed by negative-stain EM using a JEM-1011 instrument (JEOL) (Figure S2a). Quinones were extracted from the purified LH1-RC and chromatophores, and quinone contents were analyzed (Figure S3) using the methods described previously .…”

Section: Methodsmentioning

confidence: 99%

Cryo-EM Structure of the Photosynthetic LH1-RC Complex from Rhodospirillum rubrum

Tani

Kanno

et al. 2021

Biochemistry

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Rhodospirillum (Rsp.) rubrum is one of the most widely used model organisms in bacterial photosynthesis. This purple phototroph is characterized by the presence of both rhodoquinone (RQ) and ubiquinone as electron carriers and bacteriochlorophyll (BChl) a esterified at the propionic acid side chain by geranylgeraniol (BChl a G ) instead of phytol. Despite intensive efforts, the structure of the light-harvesting-reaction center (LH1-RC) core complex from Rsp. rubrum remains at low resolutions. Using cryo-EM, here we present a robust new view of the Rsp. rubrum LH1-RC at 2.76 Å resolution. The LH1 complex forms a closed, slightly elliptical ring structure with 16 αβ-polypeptides surrounding the RC. Our biochemical analysis detected RQ molecules in the purified LH1-RC, and the cryo-EM density map specifically positions RQ at the Q A site in the RC. The geranylgeraniol side chains of BChl a G coordinated by LH1 β-polypeptides exhibit a highly homologous tail-up conformation that allows for interactions with the bacteriochlorin rings of nearby LH1 αassociated BChls a G . The structure also revealed key protein−protein interactions in both Nand C-terminal regions of the LH1 αβ-polypeptides, mainly within a face-to-face structural subunit. Our high-resolution Rsp. rubrum LH1-RC structure provides new insight for evaluating past experimental and computational results obtained with this old organism over many decades and lays the foundation for more detailed exploration of light-energy conversion, quinone transport, and structure−function relationships in this pigment−protein complex.

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“…We have earlier used SHLS to study two types of binding between HSA and bilirubin . Most recently, Ma et al reported large hyperpolarizability from bacterial light harvesting complexes . But until date, there is no report on application of this technique to study protein–protein interaction.…”

Section: Introductionmentioning

confidence: 99%

“…16 Most recently, Ma et al reported large hyperpolarizability from bacterial light harvesting complexes. 17 But until date, there is no report on application of this technique to study protein−protein interaction. We have used modified Langmuir model to extract the number of Hb molecules which bind to the dimeric and tetrameric spectrin.…”

Section: ■ Introductionmentioning

confidence: 99%

Protein–Protein Interaction Probed by Label-free Second Harmonic Light Scattering: Hemoglobin Adsorption on Spectrin Surface as a Case Study

2017

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In this article, we have studied the binding of different naturally occurring hemoglobin (Hb) variants on erythrocyte skeletal protein, spectrin surface using the label free nondestructive second harmonic light scattering (SHLS) technique in aqueous buffer. Hemoglobin variants like sickle hemoglobin (HbS) and hemoglobin E (HbE) were chosen as they associate with sickle cell disease and HbEβ-thalassemia, respectively, and their interaction with spectrin is compared with normal adult hemoglobin (HbA). The concentration dependent change in the second harmonic light intensity from nanomolar spectrin solution has been measured after addition of small aliquots of hemoglobins. From the second harmonic titration data, the binding constant is calculated using a modified Langmuir adsorption model of hemoglobin binding to the spectrin surface. Interestingly, it is found that the binding constant for HbE (13.8 × 10 M) is 1 order of magnitude higher than that of HbS (1.6 × 10 M) or HbA (2.1 × 10 M) which indicates higher affinity of HbE for spectrin compared to HbA and HbS. The number of the Hb molecules bound to the spectrin surface was estimated to be of the order of hundred's which is determined for the first time.

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Bacterial Light-Harvesting Complexes Showing Giant Second-Order Nonlinear Optical Response as Revealed by Hyper-Rayleigh Light Scattering

Cited by 4 publications

References 44 publications

Biochemical and Spectroscopic Characterizations of a Hybrid Light-Harvesting Reaction Center Core Complex

Biochemical and Spectroscopic Characterizations of a Hybrid Light-Harvesting Reaction Center Core Complex

Cryo-EM Structure of the Photosynthetic LH1-RC Complex from Rhodospirillum rubrum

Protein–Protein Interaction Probed by Label-free Second Harmonic Light Scattering: Hemoglobin Adsorption on Spectrin Surface as a Case Study

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