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.

Journal Article · Fri Mar 04 00:00:00 EST 2011 · Biomolecular NMR Assignments, 5(1):89-92

DOI:https://doi.org/10.1007/s12104-010-9274-1· OSTI ID:1009303

Cort, John R; Swenson, Michael; Magnuson, Timothy S

We report the 1H, 13C, and 15N chemical shift assignments of both oxidized and reduced forms of an abundant periplasmic c-type cytochrome, designated ApcA, from the acidophilic gram-negative facultatively anaerobic metal-reducing alpha-proteobacterium Acidiphilium cryptum. These resonance assignments prove that ApcA is a monoheme cytochrome c2 and the product of the Acry_2099 gene. An absence of resonance peaks in the NMR spectra for the 21 N-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 13C- and 15N- labeled substrates.

• Research Organization: Pacific Northwest National Lab. (PNNL), Richland, WA (United States). Environmental Molecular Sciences Lab. (EMSL)
• Sponsoring Organization: USDOE
• DOE Contract Number: AC05-76RL01830
• OSTI ID: 1009303
• Report Number(s): PNNL-SA-74669; 26709; 39728; KP1704020; TRN: US201106%%509
• Journal Information: Biomolecular NMR Assignments, 5(1):89-92, Vol. 5, Issue 1
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
CHEMICAL SHIFT
CYTOCHROMES
HEME
NMR SPECTRA
PROTEINS
PURIFICATION
RESIDUES
RESONANCE
SUBSTRATES
EMSL
NMR spectroscopy
protein structure determination
microbe-mineral interface
electron transport
metal-reducing bacteria
Environmental Molecular Sciences Laboratory