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.
journal_name
Biomol NMR Assignjournal_title
Biomolecular NMR assignmentsauthors
Cort JR,Swenson MW,Magnuson TSdoi
10.1007/s12104-010-9274-1subject
Has Abstractpub_date
2011-04-01 00:00:00pages
89-92issue
1eissn
1874-2718issn
1874-270Xjournal_volume
5pub_type
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