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Structural and Functional Insights into a Lysine Deacylase in the Cyanobacterium Synechococcus sp. PCC 7002.
Title: Structural and Functional Insights into a Lysine Deacylase in the Cyanobacterium Synechococcus sp. PCC 7002.
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The role of PsbO succinylation in the bacterial growth growth, photosynthesis and electron transport.[PsbO]
Title: Effects of PSII Manganese-Stabilizing Protein Succinylation on Photosynthesis in the Model Cyanobacterium Synechococcus sp. PCC 7002.
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NrrA facilitates cell survival by activating glycogen degradation and the oxidative pentose phosphate (OPP) pathway under nitrogen-deprived conditions. [NrrA]
Title: Transcriptional Activation of Glycogen Catabolism and the Oxidative Pentose Phosphate Pathway by NrrA Facilitates Cell Survival Under Nitrogen Starvation in the Cyanobacterium Synechococcus sp. Strain PCC 7002.
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At high pH and only in the ferrous state, Lys42 competes with His46 for the iron coordination site. The reversible ligand switching has an apparent pKa of 9.3 and a Lys-ligated population of approximately 60% at the basic pH limit in the modified holoprotein. The switching rate was about 20-30 s(-1). Lys42-His46 competition and conformational rearrangement may be related to low bis-histidine ligation and more backbone ...
Title: Histidine-Lysine Axial Ligand Switching in a Hemoglobin: A Role for Heme Propionates.
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Constructed was a knockout mutant of nitrate reductase, encoded by narB, in Synechococcus sp. PCC 7002. As expected, DeltanarB was able to take up intracellular nitrate but was unable to reduce it to nitrite or ammonia, and was unable to grow photoautotrophically on nitrate. [nitrate reductase]
Title: Inactivation of nitrate reductase alters metabolic branching of carbohydrate fermentation in the cyanobacterium Synechococcus sp. strain PCC 7002.
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the increased absorption cross-section from the IsiA proteins translates directly to an enhanced rate of electron transfer through Photosystem I [IsiA]
Title: The Presence of the IsiA-PSI Supercomplex Leads to Enhanced Photosystem I Electron Throughput in Iron-Starved Cells of Synechococcus sp. PCC 7002.
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The structure of cytochrome c6C from the mesophilic cyano-bacterium Synechococcus sp. PCC 7002 has been determined at 1.03 A resolution. [cytochrome c6C]
Title: Insights into the relationship between the haem-binding pocket and the redox potential of c6 cytochromes: four atomic resolution structures of c6 and c6-like proteins from Synechococcus sp. PCC 7002.
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(1)H, (15)N, and (13)C assignments for the ferric (low-spin, S = (1/2)) protein with a b heme cofactor and after post-translational modification leading to a c-like heme. [hemoglobin]
Title: (1)H, (15)N, and (13)C resonance assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferric bis-histidine state.
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Thus, CpcM is the methyltransferase that modifies the amide nitrogen of Asn71/72 of CpcB, ApcB, and ApcF.
Title: CpcM posttranslationally methylates asparagine-71/72 of phycobiliprotein beta subunits in Synechococcus sp. strain PCC 7002 and Synechocystis sp. strain PCC 6803.
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CpcT is a new phycocyanobilin lyase that specifically attaches phycocyanobilin to Cys-153 of the phycocyanin beta-subunit[CPCT]
Title: Identification and characterization of a new class of bilin lyase: the cpcT gene encodes a bilin lyase responsible for attachment of phycocyanobilin to Cys-153 on the beta-subunit of phycocyanin in Synechococcus sp. PCC 7002.