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Title		Authors	PubMed ID
1	Enzymatic Synthesis of a Fluorogenic Reporter Substrate and the Development of a High-Throughput Assay for Fucosyltransferase VIII Provide a Toolkit to Probe and Inhibit Core Fucosylation.	Soroko M, Kwan DH	32441090 CHEMBIOCHEM
2	Identification of active site residues of chorismate mutase-prephenate dehydrogenase from Escherichia coli.	Christendat D, Turnbull J	8605196 CHEMBIOCHEM
3	Characterization of active and inactive forms of the phenol hydroxylase stimulatory protein DmpM.	Cadieux E, Powlowski J	10451366 CHEMBIOCHEM
4	S-nitrosation of Ca(2+)-loaded and Ca(2+)-free recombinant calbindin D(28K) from human brain.	Tao L, Murphy ME, English AM	11994015 CHEMBIOCHEM
5	Mechanism of S-nitrosation of recombinant human brain calbindin D28K.	Tao L, English AM	12641465 CHEMBIOCHEM
6	Protein S-glutathiolation triggered by decomposed S-nitrosoglutathione.	Tao L, English AM	15049710 CHEMBIOCHEM
7	Mass spectrometric analysis of nitroxyl-mediated protein modification: comparison of products formed with free and protein-based cysteines.	Shen B, English AM	16229492 CHEMBIOCHEM
8	A shared binding site for NAD+ and coenzyme A in an acetaldehyde dehydrogenase involved in bacterial degradation of aromatic compounds.	Lei Y, Pawelek PD, Powlowski J	18537268 CHEMBIOCHEM
9	Backbone Flexibility Influences Nucleotide Incorporation by Human Translesion DNA Polymerase η opposite Intrastrand Cross-Linked DNA.	O'Flaherty DK, Guengerich FP, Egli M, Wilds CJ	26624500 CHEMBIOCHEM
10	Proton release due to manganese binding and oxidation in modified bacterial reaction centers.	Kálmán L, Thielges MC, Williams JC, Allen JP	16201752 PHYSICS
11	Light-induced conformational changes in photosynthetic reaction centers: dielectric relaxation in the vicinity of the dimer.	Deshmukh SS, Williams JC, Allen JP, Kálmán L	21141811 PHYSICS
12	Light-induced conformational changes in photosynthetic reaction centers: redox-regulated proton pathway near the dimer.	Deshmukh SS, Williams JC, Allen JP, Kálmán L	21410139 PHYSICS
13	Light-induced conformational changes in photosynthetic reaction centers: impact of detergents and lipids on the electronic structure of the primary electron donor.	Deshmukh SS, Akhavein H, Williams JC, Allen JP, Kalman L	21561160 PHYSICS

Title:	Mechanism of S-nitrosation of recombinant human brain calbindin D28K.
Authors:	Tao L, English AM
Link:	https://www.ncbi.nlm.nih.gov/pubmed/12641465?dopt=Abstract
DOI:	10.1021/bi0269963
Publication:	Biochemistry
Keywords:
PMID:	12641465	Category:	Biochemistry	Date Added:	2019-06-20
Dept Affiliation:	CHEMBIOCHEM 1 Department of Chemistry and Biochemistry, Concordia University, 1455 de Maisonneuve Boulevard West, Montreal, Quebec, Canada H3G 1M8.

Description:

Mechanism of S-nitrosation of recombinant human brain calbindin D28K.

Biochemistry. 2003 Mar 25;42(11):3326-34

Authors: Tao L, English AM

Abstract

Mass spectrometry and UV-vis absorption results support a mechanism for NO donation by S-nitrosoglutathione (GSNO) to recombinant human brain calbindin D(28K) (rHCaBP) that requires the presence of trace copper, added as either Cu,Zn-superoxide dismutase (CuZnSOD) or CuSO(4). The extent of copper-catalyzed rHCaBP S-nitrosation depends on the ratio of protein to GSNO and on the reaction time, and NO-transfer is prevented when copper chelators are present. CuZnSOD is an efficient catalyst of rHCaBP S-nitrosation, and the mechanism of CuZnSOD-catalyzed S-nitrosation involves reduction of the active-site Cu(II) by a number of the five free thiols in rHCaBP, giving rise to thiyl radicals. The Cu(I)ZnSOD formed catalyzes the reductive cleavage of GSNO present in solution to give GSH and release NO. rHCaBP thiyl radicals react with NO to yield the S-nitrosoprotein. Cu(II)ZnSOD is also reduced by GSH in a concentration-dependent manner up to 5 mM but not at higher GSH concentrations. However, unlike the rHCaBP thiyl radicals, GS(*) radicals dimerize to GSSG faster than their reaction with NO. The data presented here provide a biologically relevant mechanism for protein S-nitrosation by small S-nitrosothiols. S-nitrosation is rapidly gaining recognition as a major form of protein posttranslational modification, and the efficient S-nitrosation of CaBP by CuZnSOD/GSNO is speculated to be of neurochemical importance given that CaBP and CuZnSOD are abundant in neurons.

PMID: 12641465 [PubMed - indexed for MEDLINE]

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