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Title: Assignment of the sup 1 H and sup 15 N NMR spectra of Rhodobacter capsulatus ferrocytochrome c sub 2

Abstract

The peptide resonances of the {sup 1}H and {sup 15}N nuclear magnetic resonance spectra of ferrocytochrome c{sub 2} from Rhodobacter capsulatus are sequentially assigned by a combination of 2D {sup 1}H-{sup 1}H and {sup 1}H-{sup 15}N spectroscopy, the latter performed on {sup 15}N-enriched protein. Short-range nuclear Overhauser effect (NOE) data show {alpha}-helices from residues 3-17, 55-65, 69-88, and 103-115. Within the latter two {alpha}-helices, there are three single 3{sub 10} turns, 70-72, 76-78, and 107-109. In addition {alpha}H-NH{sub i+1} and {alpha}H-NH{sub i+2} NOEs indicate that the N-terminal helix (3-17) is distorted. Compared to horse or tuna cytochrome c and cytochrome c{sub 2} of Rhodospirillium rubrum, there is a 6-residue insertion at residues 23-29 in R. capsulatus cytochrome c{sub 2}. The NOE data show that this insertion forms a loop, probably an {Omega} loop. {sup 1}H-{sup 15}N heteronuclear multiple quantum correlation experiments are used to follow NH exchange over a period of 40 h. As the 2D spectra are acquired in short time periods (30 min), rates for intermediate exchanging protons can be measured. Comparison of the NH exchange data for the N-terminal helix of cytochrome c{sub 2} of R. capsulatus with the highly homologous horse heart cytochrome c shows thatmore » this helix is less stable in cytochrome c{sub 2}.« less

Authors:
; ; ;  [1]
  1. (Univ. of Arizona, Tucson (USA))
Publication Date:
OSTI Identifier:
7192989
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemistry; (USA); Journal Volume: 29:9
Country of Publication:
United States
Language:
English
Subject:
62 RADIOLOGY AND NUCLEAR MEDICINE; CYTOCHROMES; NUCLEAR MAGNETIC RESONANCE; AMMONIUM SULFATES; BACTERIA; CHEMICAL SHIFT; IRON COMPOUNDS; MOLECULAR STRUCTURE; NITROGEN 15; OVERHAUSER EFFECT; PROTONS; RHODOSPIRILLUM; AMMONIUM COMPOUNDS; BARYONS; ELEMENTARY PARTICLES; FERMIONS; HADRONS; ISOTOPES; LIGHT NUCLEI; MAGNETIC RESONANCE; MICROORGANISMS; NITROGEN ISOTOPES; NUCLEI; NUCLEONS; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; OXYGEN COMPOUNDS; PIGMENTS; PROTEINS; RESONANCE; STABLE ISOTOPES; SULFATES; SULFUR COMPOUNDS; TRANSITION ELEMENT COMPOUNDS; 550601* - Medicine- Unsealed Radionuclides in Diagnostics

Citation Formats

Gooley, P.R., Caffrey, M.S., Cusanovich, M.A., and MacKenzie, N.E. Assignment of the sup 1 H and sup 15 N NMR spectra of Rhodobacter capsulatus ferrocytochrome c sub 2. United States: N. p., 1990. Web. doi:10.1021/bi00461a011.
Gooley, P.R., Caffrey, M.S., Cusanovich, M.A., & MacKenzie, N.E. Assignment of the sup 1 H and sup 15 N NMR spectra of Rhodobacter capsulatus ferrocytochrome c sub 2. United States. doi:10.1021/bi00461a011.
Gooley, P.R., Caffrey, M.S., Cusanovich, M.A., and MacKenzie, N.E. Tue . "Assignment of the sup 1 H and sup 15 N NMR spectra of Rhodobacter capsulatus ferrocytochrome c sub 2". United States. doi:10.1021/bi00461a011.
@article{osti_7192989,
title = {Assignment of the sup 1 H and sup 15 N NMR spectra of Rhodobacter capsulatus ferrocytochrome c sub 2},
author = {Gooley, P.R. and Caffrey, M.S. and Cusanovich, M.A. and MacKenzie, N.E.},
abstractNote = {The peptide resonances of the {sup 1}H and {sup 15}N nuclear magnetic resonance spectra of ferrocytochrome c{sub 2} from Rhodobacter capsulatus are sequentially assigned by a combination of 2D {sup 1}H-{sup 1}H and {sup 1}H-{sup 15}N spectroscopy, the latter performed on {sup 15}N-enriched protein. Short-range nuclear Overhauser effect (NOE) data show {alpha}-helices from residues 3-17, 55-65, 69-88, and 103-115. Within the latter two {alpha}-helices, there are three single 3{sub 10} turns, 70-72, 76-78, and 107-109. In addition {alpha}H-NH{sub i+1} and {alpha}H-NH{sub i+2} NOEs indicate that the N-terminal helix (3-17) is distorted. Compared to horse or tuna cytochrome c and cytochrome c{sub 2} of Rhodospirillium rubrum, there is a 6-residue insertion at residues 23-29 in R. capsulatus cytochrome c{sub 2}. The NOE data show that this insertion forms a loop, probably an {Omega} loop. {sup 1}H-{sup 15}N heteronuclear multiple quantum correlation experiments are used to follow NH exchange over a period of 40 h. As the 2D spectra are acquired in short time periods (30 min), rates for intermediate exchanging protons can be measured. Comparison of the NH exchange data for the N-terminal helix of cytochrome c{sub 2} of R. capsulatus with the highly homologous horse heart cytochrome c shows that this helix is less stable in cytochrome c{sub 2}.},
doi = {10.1021/bi00461a011},
journal = {Biochemistry; (USA)},
number = ,
volume = 29:9,
place = {United States},
year = {Tue Mar 06 00:00:00 EST 1990},
month = {Tue Mar 06 00:00:00 EST 1990}
}