2023
A quantitative assessment of (bacterio)chlorophyll assignments in the cryo-EM structure of the Chloracidobacterium thermophilum reaction center
Gisriel C, Flesher D, Long Z, Liu J, Wang J, Bryant D, Batista V, Brudvig G. A quantitative assessment of (bacterio)chlorophyll assignments in the cryo-EM structure of the Chloracidobacterium thermophilum reaction center. Photosynthesis Research 2023, 1-10. PMID: 37749456, DOI: 10.1007/s11120-023-01047-5.Peer-Reviewed Original ResearchCryo-EM mapsCryogenic electron microscopy structureReaction centersHydrogen bond donorCryo-EM structureElectron microscopy structureReaction center complexBond donorPhotosynthetic organismsMicroscopy structureProtein complexesElectron transferMolecular structureFunctional insightsStructural biologyLight harvestingProtein environmentChemical environmentExperimental cryo-EM mapsDownstream investigationsCenter complexPrimary pigmentEnergy transferStructural dataAcetyl moiety
2017
Chlorophyll a with a farnesyl tail in thermophilic cyanobacteria
Wiwczar JM, LaFountain AM, Wang J, Frank HA, Brudvig GW. Chlorophyll a with a farnesyl tail in thermophilic cyanobacteria. Photosynthesis Research 2017, 134: 175-182. PMID: 28741056, PMCID: PMC5832022, DOI: 10.1007/s11120-017-0425-4.Peer-Reviewed Original ResearchConceptsThermophilic cyanobacteriaPhotosystem IIMajor light-harvesting pigmentOxygenic photosynthetic organismsLight-harvesting pigmentsÅ crystal structurePhotosynthetic organismsFarnesyl tailCyanobacteriaIsoprene unitsSpecific ChlSmall populationPhytyl tailElectron density mapsTailChlMass spectrometryOrganismsCofactorDensity mapsCrystal structureHigh-performance liquid chromatographyExperimental evidencePigmentsLiquid chromatography
1999
New insights into the ATP‐dependent Clp protease: Escherichia coli and beyond
Porankiewicz J, Wang J, Clarke A. New insights into the ATP‐dependent Clp protease: Escherichia coli and beyond. Molecular Microbiology 1999, 32: 449-458. PMID: 10320569, DOI: 10.1046/j.1365-2958.1999.01357.x.Peer-Reviewed Original ResearchConceptsClp proteaseClpP proteinATP-dependent Clp proteaseClp/Hsp100Escherichia coliKey metabolic enzymesPrecise regulatory mechanismsChaperone subunitsPhotosynthetic organismsHigher plantsRegulatory subunitCellular processesHeptameric ringsHexameric ringThree-dimensional structureProteolytic subunitNew insightsRegulatory mechanismsProtein turnoverMetabolic enzymesFunctional importanceSubunitsProteaseRecent findingsProtein