PERFORM Publications

Keyword search (4,163 papers available)

Title		Authors	PubMed ID
1	Mass spectral analysis of protein-based radicals using DBNBS. Nonradical adduct formation versus spin trapping.	Filosa A, English AM	11262405 CHEMBIOCHEM
2	Heme nitrosylation of deoxyhemoglobin by s-nitrosoglutathione requires copper.	Romeo AA, Capobianco JA, English AM	11970954 CHEMBIOCHEM
3	Biochemical and molecular characterization of a hydroxyjasmonate sulfotransferase from Arabidopsis thaliana.	Gidda SK, Miersch O, Levitin A, Schmidt J, Wasternack C, Varin L	12637544 BIOLOGY
4	The evolutionary rewiring of the ribosomal protein transcription pathway modifies the interaction of transcription factor heteromer Ifh1-Fhl1 (interacts with forkhead 1-forkhead-like 1) with the DNA-binding specificity element.	Mallick J, Whiteway M	23625919 BIOLOGY
5	Discovery and characterization of family 39 glycoside hydrolases from rumen anaerobic fungi with polyspecific activity on rare arabinosyl substrates.	Jones DR, Uddin MS, Gruninger RJ, Pham TTM, Thomas D, Boraston AB, Briggs J, Pluvinage B, McAllister TA, Forster RJ, Tsang A, Selinger LB, Abbott DW	28588026 CSFG

Title:	Heme nitrosylation of deoxyhemoglobin by s-nitrosoglutathione requires copper.
Authors:	Romeo AA, Capobianco JA, English AM
Link:	https://www.ncbi.nlm.nih.gov/pubmed/11970954?dopt=Abstract
DOI:	10.1074/jbc.M202221200
Publication:	The Journal of biological chemistry
Keywords:
PMID:	11970954	Category:	J Biol Chem	Date Added:	2019-06-20
Dept Affiliation:	CHEMBIOCHEM 1 Department of Chemistry and Biochemistry, Concordia University, 1455 de Maisonneuve Boulevard West, Montreal, Quebec H3G 1M8, Canada.

Description:

Heme nitrosylation of deoxyhemoglobin by s-nitrosoglutathione requires copper.

J Biol Chem. 2002 Jul 05;277(27):24135-41

Authors: Romeo AA, Capobianco JA, English AM

Abstract

NO reactions with hemoglobin (Hb) likely play a role in blood pressure regulation. For example, NO exchange between Hb and S-nitrosoglutathione (GSNO) has been reported in vitro. Here we examine the reaction between GSNO and deoxyHb (HbFe(II)) in the presence of both Cu(I) (2,9-dimethyl-1, 10-phenanthroline (neocuproine)) and Cu(II) (diethylenetriamine-N,N,N',N",N"-pentaacetic acid) chelators using a copper-depleted Hb solution. Spectroscopic analysis of deoxyHb (HbFe(II))/GSNO incubates shows prompt formation (<5 min) of approximately 100% heme-nitrosylated Hb (HbFe(II)NO) in the absence of chelators, 46% in the presence of diethylenetriamine-N,N,N',N",N"-pentaacetic acid, and 25% in the presence of neocuproine. Negligible (<2%) HbFe(II)NO was detected when neocuproine was added to copper-depleted HbFe(II)/GSNO incubates. Thus, HbFe(II)NO formation via a mechanism involving free NO generated by Cu(I) catalysis of GSNO breakdown is proposed. GSH is a source of reducing equivalents because extensive GSSG was detected in HbFe(II)/GSNO incubates in the absence of metal chelators. No S-nitrosation of HbFe(II) was detected under any conditions. In contrast, the NO released from GSNO is directed to Cysbeta(93) of oxyHb in the absence of chelators, but only metHb formation is observed in the presence of chelators. Our findings reveal that the reactions of GSNO and Hb are controlled by copper and that metal chelators do not fully inhibit NO release from GSNO in Hb-containing solutions.

PMID: 11970954 [PubMed - indexed for MEDLINE]

BookR: School of Health Core Facilities Booking

"J Biol Chem" Category Publications:

Search Publications

No results