Structural Analysis of the Homodimeric Reaction Center Complex from the Photosynthetic Green Sulfur Bacterium <i>Chlorobaculum tepidum</i>

He, Guannan; Zhang, Hao; King, Jeremy D.; Blankenship, Robert E.

doi:10.1021/bi5006464

Cited by 34 publications

(36 citation statements)

References 39 publications

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“…In fact, this is the only position where Cytochrome c 551 could bind so that the cytoplasmic domain, which contains the heme, can be positioned near P840 on the periplasmic side of the membrane. This location is also consistent with recent cross-linking experiments done with isolated reaction centers (He et al, 2014 ). Are these incredible cases of molecular convergent evolution or was the ancestral reaction center to Photosystem I and Photosystem II more complex than previously anticipated?…”

Section: The Ancient Recruitment Of Additional Protein Subunitssupporting

confidence: 92%

“…In fact, like D1 and D2, PsaA and PsaB also have an extension of the protein sequence in between the equivalent transmembrane helices 7th and 8th (homologous to 1st and 2nd in Type II) that interacts with PsaL and PsaFJ, see Figure 4 . Additionally, in the cross-linking experiment mentioned above, the PscA subunit from the reaction center of Chlorobaculum tepidum cross-linked with the Cytochrome c 551 via a lysine also found in between the 7th and 8th helices (He et al, 2014 ). All in all, it is a strong indication that the primordial reaction center A was interacting with membrane bound proteins, regardless of their original function.…”

Section: The Ancient Recruitment Of Additional Protein Subunitsmentioning

confidence: 99%

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Reconstructing the Origin of Oxygenic Photosynthesis: Do Assembly and Photoactivation Recapitulate Evolution?

Cardona

2016

Front. Plant Sci.

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Due to the great abundance of genomes and protein structures that today span a broad diversity of organisms, now more than ever before, it is possible to reconstruct the molecular evolution of protein complexes at an incredible level of detail. Here, I recount the story of oxygenic photosynthesis or how an ancestral reaction center was transformed into a sophisticated photochemical machine capable of water oxidation. First, I review the evolution of all reaction center proteins in order to highlight that Photosystem II and Photosystem I, today only found in the phylum Cyanobacteria, branched out very early in the history of photosynthesis. Therefore, it is very unlikely that they were acquired via horizontal gene transfer from any of the described phyla of anoxygenic phototrophic bacteria. Second, I present a new evolutionary scenario for the origin of the CP43 and CP47 antenna of Photosystem II. I suggest that the antenna proteins originated from the remodeling of an entire Type I reaction center protein and not from the partial gene duplication of a Type I reaction center gene. Third, I highlight how Photosystem II and Photosystem I reaction center proteins interact with small peripheral subunits in remarkably similar patterns and hypothesize that some of this complexity may be traced back to the most ancestral reaction center. Fourth, I outline the sequence of events that led to the origin of the Mn4CaO5 cluster and show that the most ancestral Type II reaction center had some of the basic structural components that would become essential in the coordination of the water-oxidizing complex. Finally, I collect all these ideas, starting at the origin of the first reaction center proteins and ending with the emergence of the water-oxidizing cluster, to hypothesize that the complex and well-organized process of assembly and photoactivation of Photosystem II recapitulate evolutionary transitions in the path to oxygenic photosynthesis.

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Section: The Ancient Recruitment Of Additional Protein Subunitssupporting

confidence: 92%

Section: The Ancient Recruitment Of Additional Protein Subunitsmentioning

confidence: 99%

Reconstructing the Origin of Oxygenic Photosynthesis: Do Assembly and Photoactivation Recapitulate Evolution?

Cardona

2016

Front. Plant Sci.

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“…The FMO-RCC complex was purified from the green sulfur bacterium Chlorobaculum tepidum strain TLS as previously reported. 31 The RCC complex was purified by a similar method with some modifications. Instead of loading onto a DEAE-cellulose column, the dark green band obtained from the centrifugation in the sucrose gradient was treated with 0.4 M Na 2 CO 3 overnight and subsequently loaded onto a hydroxyapatite column of about 10 mL bed volume.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

Dynamics of Energy and Electron Transfer in the FMO-Reaction Center Core Complex from the Phototrophic Green Sulfur Bacterium Chlorobaculum tepidum

Niedzwiedzki

Orf

et al. 2015

J. Phys. Chem. B

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The reaction center core (RCC) complex and the RCC with associated Fenna-Matthews-Olson protein (FMO-RCC) complex from the green sulfur bacterium Chlorobaculum tepidum were studied comparatively by steady-state and time-resolved fluorescence (TRF) and femtosecond time-resolved transient absorption (TA) spectroscopies. The energy transfer efficiency from the FMO to the RCC complex was calculated to be ∼40% based on the steady-state fluorescence. TRF showed that most of the FMO complexes (66%), regardless of the fact that they were physically attached to the RCC, were not able to transfer excitation energy to the reaction center. The TA spectra of the RCC complex showed a 30-38 ps lifetime component regardless of the excitation wavelengths, which is attributed to charge separation. Excitonic equilibration was shown in TA spectra of the RCC complex when excited into the BChl a Qx band at 590 nm and the Chl a Qy band at 670 nm, while excitation at 840 nm directly populated the low-energy excited state and equilibration within the excitonic BChl a manifold was not observed. The TA spectra for the FMO-RCC complex excited into the BChl a Qx band could be interpreted by a combination of the excited FMO protein and RCC complex. The FMO-RCC complex showed an additional fast kinetic component compared with the FMO protein and the RCC complex, which may be due to FMO-to-RCC energy transfer.

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“…The architecture of phycobilisomes from Thermosynechococcus vulcanus was also studied by crosslinking [95]. Finally, the complex between the Fenna-Matthews-Olson antenna protein and the reaction center core complex in Chlorobaculum tepidum was also probed by XL-MS [96].…”

Section: Box 1 Crosslinking Of Protein Network and Whole Proteomesmentioning

confidence: 99%

Crosslinking and Mass Spectrometry: An Integrated Technology to Understand the Structure and Function of Molecular Machines

Leitner

Faini

Stengel

et al. 2016

Trends in Biochemical Sciences

348

285

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In recent years, chemical crosslinking of protein complexes and the identification of crosslinked residues by mass spectrometry (XL-MS; sometimes abbreviated as CX-MS) has become an important technique bridging mass spectrometry (MS) and structural biology. By now, XL-MS is well established and supported by publicly available resources as a convenient and versatile part of the structural biologist's toolbox. The combination of XL-MS with cryoelectron microscopy (cryo-EM) and/or integrative modeling is particularly promising to study the topology and structure of large protein assemblies. Among the targets studied so far are proteasomes, ribosomes, polymerases, chromatin remodelers, and photosystem complexes. Here we provide an overview of recent advances in XL-MS, the current state of the field, and a cursory outlook on future challenges. Chemical Crosslinking as a Tool for Structural BiologyStructural biology makes use of many different techniques to elucidate the 3D structures of proteins and protein complexes. While high-resolution structures have traditionally been obtained by X-ray crystallography, cryo-EM is increasingly able to also generate (near) atomic-resolution models. In recent years, techniques and applications of MS have also rapidly progressed. Earlier studies were largely focused on the large-scale identification and quantification of proteins, whereas recent methods also support queries into the composition, stoichiometry, and spatial arrangement of subunits in a complex. These developments have now further progressed toward generating information that contributes, as part of hybrid structural strategies, to the structure elucidation of large molecular assemblies including protein complexes that perform essential processes in the cell. XL-MS is a particularly powerful mass spectrometric technique in this respect, because it provides several layers of information. Identifying protein-protein contacts through XL-MS confirms physical proximity between subunits because the proteins must be close enough in space to be crosslinked. Localizing the side chains that are connected restricts this proximity to certain regions (e.g., domains or even single helices or loops). Finally, the structure of the connected side chains and the crosslinker moiety impart a distance restraint that can be used for molecular modeling purposes because an upper Trends Chemical crosslinking followed by the mass spectrometric analysis of cross linked peptides (XL MS) identifies con tact sites between residues within a single or between multiple proteins.The application of XL MS to many bio logically relevant molecular machines has been shown, with a rapidly growing number of successful studies reported in the past 2 3 years.Crosslinking data are useful in integra tive modeling workflows by providing distance restraints on the surface of folded proteins and complexes. XL MS has been shown to be particularly powerful in combination with 3D cryo electron microscopy. Sciences ; 41 (2016), 1. -S. 20-32 https://dx.doi.org/10.1016...

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Structural Analysis of the Homodimeric Reaction Center Complex from the Photosynthetic Green Sulfur Bacterium Chlorobaculum tepidum

Cited by 34 publications

References 39 publications

Reconstructing the Origin of Oxygenic Photosynthesis: Do Assembly and Photoactivation Recapitulate Evolution?

Reconstructing the Origin of Oxygenic Photosynthesis: Do Assembly and Photoactivation Recapitulate Evolution?

Dynamics of Energy and Electron Transfer in the FMO-Reaction Center Core Complex from the Phototrophic Green Sulfur Bacterium Chlorobaculum tepidum

Crosslinking and Mass Spectrometry: An Integrated Technology to Understand the Structure and Function of Molecular Machines

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