Search Results - "Falzone, Christopher J."
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Functional and Structural Characterization of the 2/2 Hemoglobin from Synechococcus sp. PCC 7002
Published in Biochemistry (Easton) (24-08-2010)“…Cyanobacterium Synechococcus sp. PCC 7002 contains a single gene (glbN) coding for GlbN, a protein of the 2/2 hemoglobin lineage. The precise function of GlbN…”
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The Solution Structure of the Recombinant Hemoglobin from the Cyanobacterium Synechocystis sp. PCC 6803 in its Hemichrome State
Published in Journal of molecular biology (13-12-2002)“…The product of the cyanobacterium Synechocystis sp. PCC 6803 gene slr2097 is a 123 amino acid polypeptide chain belonging to the truncated hemoglobin family…”
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Truncated Hemoglobin from the Cyanobacterium Synechococcus sp. PCC 7002: Evidence for Hexacoordination and Covalent Adduct Formation in the Ferric Recombinant Protein
Published in Biochemistry (Easton) (04-06-2002)“…The glbN gene for the hemoglobin of Synechoccocus sp. PCC 7002, a cyanobacterium incapable of nitrogen fixation, was cloned and overexpressed in Escherichia…”
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Binding of Ferric Heme by the Recombinant Globin from the Cyanobacterium Synechocystis sp. PCC 6803
Published in Biochemistry (Easton) (29-05-2001)“…The product of the cyanobacterium Synechocystis sp. PCC 6803 gene slr2097 is a 123 amino acid polypeptide chain belonging to the truncated hemoglobin family…”
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5
Dynamics of a flexible loop in dihydrofolate reductase from Escherichia coli and its implication for catalysis
Published in Biochemistry (Easton) (18-01-1994)“…Apo-dihydrofolate reductase from Escherichia coli samples two distinct environments slowly on the NMR time scale at room temperature. Several assigned…”
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Functional role of a mobile loop of Escherichia coli dihydrofolate reductase in transition-state stabilization
Published in Biochemistry (Easton) (01-09-1992)“…The function of a highly mobile loop in Escherichia coli dihydrofolate reductase was studied by constructing a mutant (DL1) using cassette mutagenesis that had…”
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The Solution Structure of Photosystem I Accessory Protein E from the Cyanobacterium Nostoc sp. Strain PCC 8009
Published in Biochemistry (Easton) (12-10-1999)“…PsaE is a small basic subunit located on the stromal (cytoplasmic) side of photosystem I. In cyanobacteria, this subunit participates in cyclic electron…”
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Chemical rescue of a site-modified ligand to a [4Fe–4S] cluster in PsaC, a bacterial-like dicluster ferredoxin bound to Photosystem I
Published in Biochimica et biophysica acta (01-06-2007)“…Chemical rescue of site-modified amino acids using externally supplied organic molecules represents a powerful method to investigate structure–function…”
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Structural and Dynamic Repercussions of Heme Binding and Heme−Protein Cross-linking in Synechococcus sp. PCC 7002 Hemoglobin
Published in Biochemistry (Easton) (28-11-2006)“…The recombinant two-on-two hemoglobin from the cyanobacterium Synechoccocus sp. PCC 7002 (S7002 rHb) is a bishistidine hexacoordinate globin capable of forming…”
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Isolation and Characterization of a Family of Stable RNA Tetraloops with the Motif YNMG That Participate in Tertiary Interactions
Published in Biochemistry (Easton) (08-10-2002)“…RNA is known to fold into a variety of structural elements, many of which have sufficient sequence complexity to make the thermodynamic study of each possible…”
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Partial NMR assignments and secondary structure mapping of the isolated α subunit of Escherichia coli tryptophan synthase, a 29‐kD TIM barrel protein
Published in Protein science (01-01-2003)“…The α subunit of tryptophan synthase (αTS) from S. typhimurium belongs to the triosephosphate isomerase (TIM) or the (β/α)8 barrel fold, one of the most common…”
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Cyanide Binding to Hexacoordinate Cyanobacterial Hemoglobins: Hydrogen-Bonding Network and Heme Pocket Rearrangement in Ferric H117A Synechocystis Hemoglobin
Published in Biochemistry (Easton) (05-10-2004)“…The truncated hemoglobin (Hb) from the cyanobacterium Synechocystis sp. PCC 6803 is a bis-histidyl hexacoordinate complex in the absence of exogenous ligands…”
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(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
Published in Biomolecular NMR assignments (01-12-2009)“…The hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 is a monomeric 123-residue Group I 2/2 hemoglobin. Here, we report (1)H, (15)N, and (13)C…”
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Characterization of the heme-histidine cross-link in cyanobacterial hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002
Published in Journal of biological inorganic chemistry (01-03-2004)“…The recombinant product of the hemoglobin gene of the cyanobacterium Synechocystis sp. PCC 6803 forms spontaneously a covalent bond linking one of the heme…”
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Structural and dynamic properties of Synechocystis sp. PCC 6803 Hb revealed by reconstitution with Zn-protoporphyrin IX
Published in Journal of inorganic biochemistry (01-08-2005)“…In its resting state, the truncated globin of the cyanobacterium Synechocystis sp. PCC 6803 exhibits hexacoordination of the heme iron, with His46 (E10) and…”
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Conformational properties of native sperm whale apomyoglobin in solution
Published in Protein science (01-07-1999)“…Apomyoglobin from sperm whale is often used for studies of ligand binding, protein folding, and protein stability. In an effort to describe its conformational…”
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Structural and Dynamic Perturbations Induced by Heme Binding in Cytochrome b5
Published in Biochemistry (Easton) (17-04-2001)“…The water-soluble domain of rat hepatic cytochrome b(5) undergoes marked structural changes upon heme removal. The solution structure of apocytochrome b(5)…”
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1H, 15N, and 13C resonance assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferric bis-histidine state
Published in Biomolecular NMR assignments (01-12-2009)“…The hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 is a monomeric 123-residue Group I 2/2 hemoglobin. Here, we report 1 H, 15 N, and 13 C…”
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19
Backbone Dynamics of Apocytochrome b5 in Its Native, Partially Folded State
Published in Biochemistry (Easton) (23-02-1999)“…The backbone dynamics in the native state of apocytochrome b5 were studied using 15N nuclear magnetic spin relaxation measurements. The field (11.7 and 14.1 T)…”
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Backbone Dynamics of Apocytochrome b 5 in Its Native, Partially Folded State
Published in Biochemistry (Easton) (20-07-1999)Get full text
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