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.

journal_name

Biomol NMR Assign

authors

Cort JR,Swenson MW,Magnuson TS

doi

10.1007/s12104-010-9274-1

subject

Has Abstract

pub_date

2011-04-01 00:00:00

pages

89-92

issue

1

eissn

1874-2718

issn

1874-270X

journal_volume

5

pub_type

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