Related ArticlesNMR study of histidine metabolism during alcoholic and malolactic fermentations of wine and their influence on histamine production.
J Agric Food Chem. 2013 Oct 2;61(39):9464-9
Authors: López-Rituerto E, Avenoza A, Busto JH, Peregrina JM
Abstract
The metabolic pathways of amino acids play a crucial role in the organoleptic and hygienic quality in wines. In particular, histidine is one of the most studied amino acids of wines due to histamine toxicity in humans, a biogenic amine derived from histidine by enzymatic decarboxylation. The development of new tools to increase knowledge on metabolism that produces histamine in wine is critical. This study investigated by using nuclear magnetic resonance (NMR) spectroscopy the transformation of histidine into histaminol and histamine during alcoholic and malolactic fermentations. The transformations of histidine into histaminol during alcoholic fermentation and into histamine during malolactic fermentation were observed. This paper highlights the importance of selecting lactic acid bacteria for malolactic fermentation to avoid the production of biogenic amines such as histamine.
Reproducibility study for free-breathing measurements of pyruvate metabolism using hyperpolarized 13C in the heart
From The DNP-NMR Blog:
Reproducibility study for free-breathing measurements of pyruvate metabolism using hyperpolarized 13C in the heart
Lau, A.Z., et al., Reproducibility study for free-breathing measurements of pyruvate metabolism using hyperpolarized (13) C in the heart. Magn Reson Med, 2013. 69(4): p. 1063-71.
http://www.ncbi.nlm.nih.gov/pubmed/22760647
nmrlearner
News from NMR blogs
0
03-17-2014 07:23 PM
A study on the influence of fast amide exchange on the accuracy of 15N relaxation rate constants
A study on the influence of fast amide exchange on the accuracy of 15N relaxation rate constants
Abstract 15N relaxation rates of amide moieties provide insight both into global as well as local backbone dynamics of peptides and proteins. As the differences in the relaxation rates in general are small, their accurate determination is of prime importance. One potential source of error is fast amide exchange. It is well known that in its presence the effects of saturation transfer and H/D exchange may result in erroneous apparent relaxation rates R 1 and R 2. Here, the extent of...
nmrlearner
Journal club
0
11-14-2012 08:07 AM
The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima
The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima
Abstract The bacterial histidine autokinase CheA contains a histidine phosphotransfer (Hpt) domain that accepts a phosphate from the catalytic domain and donates the phosphate to either target response regulator protein, CheY or CheB. The Hpt domain forms a helix-bundle structure with a conserved four-helix bundle motif and a variable fifth helix. Observation of two nearly equally populated conformations in the crystal...
nmrlearner
Journal club
0
09-30-2011 08:01 PM
Protonation, Tautomerization, and Rotameric Structure of Histidine: A Comprehensive Study by Magic-Angle-Spinning Solid-State NMR.
Protonation, Tautomerization, and Rotameric Structure of Histidine: A Comprehensive Study by Magic-Angle-Spinning Solid-State NMR.
Protonation, Tautomerization, and Rotameric Structure of Histidine: A Comprehensive Study by Magic-Angle-Spinning Solid-State NMR.
J Am Chem Soc. 2011 Jan 5;
Authors: Li S, Hong M
Histidine structure and chemistry lie at the heart of many enzyme active sites, ion channels, and metalloproteins. While solid-state NMR spectroscopy has been used to study histidine chemical shifts, the full pH dependence of the...
nmrlearner
Journal club
0
01-07-2011 11:21 PM
Protonation, Tautomerization, and Rotameric Structure of Histidine: A Comprehensive Study by Magic-Angle-Spinning Solid-State NMR
Protonation, Tautomerization, and Rotameric Structure of Histidine: A Comprehensive Study by Magic-Angle-Spinning Solid-State NMR
Shenhui Li and Mei Hong
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja108943n/aop/images/medium/ja-2010-08943n_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/ja108943n
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/FuFM0C9qHyE
nmrlearner
Journal club
0
01-05-2011 11:40 PM
[NMR paper] 15N and 1H NMR study of histidine containing protein (HPr) from Staphylococcus carnos
15N and 1H NMR study of histidine containing protein (HPr) from Staphylococcus carnosus at high pressure.
Related Articles 15N and 1H NMR study of histidine containing protein (HPr) from Staphylococcus carnosus at high pressure.
Protein Sci. 2000 Apr;9(4):693-703
Authors: Kalbitzer HR, Görler A, Li H, Dubovskii PV, Hengstenberg W, Kowolik C, Yamada H, Akasaka K
The pressure-induced changes in 15N enriched HPr from Staphylococcus carnosus were investigated by two-dimensional (2D) heteronuclear NMR spectroscopy at pressures ranging from...
nmrlearner
Journal club
0
11-18-2010 09:15 PM
[NMR paper] Solution (1)H NMR study of the influence of distal hydrogen bonding and N terminus ac
Solution (1)H NMR study of the influence of distal hydrogen bonding and N terminus acetylation on the active site electronic and molecular structure of Aplysia limacina cyanomet myoglobin.
Related Articles Solution (1)H NMR study of the influence of distal hydrogen bonding and N terminus acetylation on the active site electronic and molecular structure of Aplysia limacina cyanomet myoglobin.
J Biol Chem. 2000 Jan 14;275(2):742-51
Authors: Nguyen BD, Xia Z, Cutruzzolá F, Allocatelli CT, Brunori M, La Mar GN
The sea hare Aplysia limacina...
nmrlearner
Journal club
0
11-18-2010 09:15 PM
[NMR paper] 1H NMR study of the influence of hydrophobic contacts on protein-prosthetic group rec
1H NMR study of the influence of hydrophobic contacts on protein-prosthetic group recognition in bovine and rat ferricytochrome b5.
Related Articles 1H NMR study of the influence of hydrophobic contacts on protein-prosthetic group recognition in bovine and rat ferricytochrome b5.
Biochemistry. 1990 Oct 16;29(41):9623-31
Authors: Lee KB, La Mar GN, Kehres LA, Fujinari EM, Smith KM, Pochapsky TC, Sligar SG
The proton nuclear magnetic resonance spectra of the soluble fragment of native bovine and genetically engineered wild-type rat...