title: 1H, 13C, and 15N backbone, side-chain, and heme chemical shift assignments for oxidized and reduced forms of the monoheme c-type cytochrome ApcA isolated from the acidophilic metal-reducing bacterium Acidiphilium cryptum.
abstract: We report the (1)H, (13)C, and (15)N chemical shift assignments of both oxidized and reduced forms of an abundant periplasmic c-type cytochrome, designated ApcA, isolated from the acidophilic gram-negative facultatively anaerobic metal-reducing alphaproteobacterium Acidiphilium cryptum. These resonance assignments prove that ApcA is a monoheme cytochrome c (2) and the product of the Acry_2099 gene. An absence of resonance peaks in the NMR spectra for the 21N-terminal residues suggests that a predicted N-terminal signal sequence is cleaved. We also describe the preparation and purification of the protein in labeled form from laboratory cultures of A. cryptum growing on (13)C- and (15)N- labeled substrates.
authors.affiliation: Biological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352, USA. john.cort@pnl.gov
authors.forename: John R
authors.initials: JR
authors.lastname: Cort
authors.forename: Michael W
authors.initials: MW
authors.lastname: Swenson
authors.forename: Timothy S
authors.initials: TS
authors.lastname: Magnuson
mesh_terms: D041801:Acidiphilium / Q000378:metabolism*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D002247:Carbon Isotopes; D003574:Cytochrome c Group / Q000737:chemistry* / Q000302:isolation & purification*; D006418:Heme / Q000737:chemistry*; D006859:Hydrogen; D008670:Metals / Q000378:metabolism*; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction
chemical_list: D001426:Bacterial Proteins; D002247:Carbon Isotopes; D003574:Cytochrome c Group; D008670:Metals; D009587:Nitrogen Isotopes; D006418:Heme; D006859:Hydrogen