Literature DB >> 5450695

Double nuclear magnetic resonance observation of electron exchange between ferri- and ferrocytochrome c.

R K Gupta, A G Redfield.   

Abstract

Cyanide-inhibited electron exchange between ferri- and ferrocytochrome c molecules has been observed by nuclear magnetic resonance. Irradiation of a partially reduced protein solution at resonance frequencies arising from protons of the oxidized state results in a decrease in the absorption due to the corresponding protons of the reduced state. The experiment quantitates the hyperfine shifts observed in this system and can be used to identify hitherto unassignable resonances. Analysis of the shifts suggests that an aromatic side chain ring lies near the edge of the heme ring.

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Year:  1970        PMID: 5450695     DOI: 10.1126/science.169.3951.1204

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  11 in total

1.  A 2D ¹³C-CEST experiment for studying slowly exchanging protein systems using methyl probes: an application to protein folding.

Authors:  Guillaume Bouvignies; Lewis E Kay
Journal:  J Biomol NMR       Date:  2012-06-12       Impact factor: 2.835

2.  NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers.

Authors:  Ashok Sekhar; Lewis E Kay
Journal:  Proc Natl Acad Sci U S A       Date:  2013-07-18       Impact factor: 11.205

Review 3.  Experimental and theoretical analysis of the interaction between cytochrome c and cytochrome b5.

Authors:  A G Mauk; M R Mauk; G R Moore; S H Northrup
Journal:  J Bioenerg Biomembr       Date:  1995-06       Impact factor: 2.945

Review 4.  Probing conformational dynamics in biomolecules via chemical exchange saturation transfer: a primer.

Authors:  Pramodh Vallurupalli; Ashok Sekhar; Tairan Yuwen; Lewis E Kay
Journal:  J Biomol NMR       Date:  2017-03-19       Impact factor: 2.835

5.  Structural studies of of "active complex" of bleomycin: assignment of ligands to the ferrous ion in a ferrous-bleomycin-carbon monoxide complex.

Authors:  N J Oppenheimer; L O Rodriguez; S M Hecht
Journal:  Proc Natl Acad Sci U S A       Date:  1979-11       Impact factor: 11.205

6.  Longitudinal relaxation optimized amide 1H-CEST experiments for studying slow chemical exchange processes in fully protonated proteins.

Authors:  Tairan Yuwen; Lewis E Kay
Journal:  J Biomol NMR       Date:  2017-03-29       Impact factor: 2.835

7.  Visualizing transient dark states by NMR spectroscopy.

Authors:  Nicholas J Anthis; G Marius Clore
Journal:  Q Rev Biophys       Date:  2015-02       Impact factor: 5.318

8.  Rates of enzyme-catalyzed exchange determined by two-dimensional NMR: a study of glucose 6-phosphate anomerization and isomerization.

Authors:  R S Balaban; J A Ferretti
Journal:  Proc Natl Acad Sci U S A       Date:  1983-03       Impact factor: 11.205

9.  31P nuclear magnetic resonance kinetic measurements on adenylatekinase.

Authors:  T R Brown; S Ogawa
Journal:  Proc Natl Acad Sci U S A       Date:  1977-09       Impact factor: 11.205

10.  31P nuclear magnetic resonance measurements of ATPase kinetics in aerobic Escherichia coli cells.

Authors:  T R Brown; K Ugurbil; R G Shulman
Journal:  Proc Natl Acad Sci U S A       Date:  1977-12       Impact factor: 11.205

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