Výsledky vyhledávání - "Shirley Tesh"

Effects of S-Nitrosation on Oxygen Binding by Normal and Sickle Cell Hemoglobin

Autor: Celia Bonaventura, Shirley Tesh, Giulia Ferruzzi, Robert Stevens

Publikováno v: Journal of Biological Chemistry. 274:24742-24748

S-Nitrosated hemoglobin (SNO-Hb) is of interest because of the allosteric control of NO delivery from SNO-Hb made possible by the conformational differences between the R- and T-states of Hb. To better understand SNO-Hb, the oxygen binding properties

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cdb3a7394fa0253063906b01f26d073
https://doi.org/10.1074/jbc.274.35.24742

Zobrazit plný text záznamu

Responses of normal and sickle cell hemoglobin to S-nitroscysteine: implications for therapeutic applications of NO in treatment of sickle cell disease

Autor: Shirley Tesh, Giulia Ferruzzi, Robert W. Henkens, Gerald Godette, Celia Bonaventura, Robert Stevens

Publikováno v: Biophysical chemistry. 98(1-2)

Factors which govern transnitrosation reactions between hemoglobin (Hb) and low molecular weight thiols may define the extent to which S-nitrosated Hb (SNO-Hb) plays a role in NO in the control of blood pressure and other NO-dependent reactions. We s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f18afe54cf6cf5354ceb9982286fb69
https://pubmed.ncbi.nlm.nih.gov/12128197

Zobrazit plný text záznamu

Disulfide bond reduction: A powerful, chemical probe for the study of structure-function relationships in the hemocyanins

Autor: Celia Bonaventura, Amy Westcott, Gregory Cole, Danielle Mercatante, Shirley Tesh, Richard W. Topham, Greer Kaufman

Publikováno v: Archives of biochemistry and biophysics. 369(2)

The copper-containing hemocyanins are a class of oxygen-transport proteins whose structures differ in arthropods and molluscs. Crystal structure analyses and amino acid sequence comparisons show that disulfide bonding is a common feature in both arth

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d3f6eced52ec522d333d04b57bd0886
https://pubmed.ncbi.nlm.nih.gov/10486145

Zobrazit plný text záznamu

Internal electron transfer between hemes and Cu(II) bound at cysteine beta93 promotes methemoglobin reduction by carbon monoxide

Autor: Linda L. Pearce, David E. Holm, Celia Bonaventura, Jim Peterson, Shirley Tesh, Alvin L. Crumbliss, Joseph Bonaventura, Gerald Godette

Publikováno v: The Journal of biological chemistry. 274(9)

Previous studies showed that CO/H2O oxidation provides electrons to drive the reduction of oxidized hemoglobin (metHb). We report here that Cu(II) addition accelerates the rate of metHb beta chain reduction by CO by a factor of about 1000. A mechanis

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::556164cca188a67081687256acf5700e
https://pubmed.ncbi.nlm.nih.gov/10026163

Zobrazit plný text záznamu

Active-site disruption in native Limulus hemocyanin and its subunits by disulfide-bond reductants: a chemical probe for the study of structure-function relationships in the hemocyanins

Autor: Richard W. Topham, Celia Bonaventura, Amy Westcott, Gregory Cole, Shirley Tesh, Danielle Mercatante

Publikováno v: Archives of biochemistry and biophysics. 352(1)

The crystal structure analysis of Subunit II of Limulus hemocyanin has shown that its polypeptide chain is folded into three distinct structural domains. The oxygen-binding, dinuclear copper center is located deep in the core of Domain 2. Two disulfi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::523a515ed662b591553f304f6ebbb2d2
https://pubmed.ncbi.nlm.nih.gov/9521822

Zobrazit plný text záznamu

Active-site heterogeneity in Limulus hemocyanin as revealed by reaction with peroxides

Autor: Shirley Tesh, Celia Bonaventura, Joseph Bonaventura, Richard W. Topham

Publikováno v: Archives of Biochemistry and Biophysics. 261:299-311

Previously reported differences in the reactivities toward active-site ligands such as hydrogen peroxide indicate that the active-site geometries of the arthropod and mollusc hemocyanins are significantly different. Results are presented which demons

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::91f0433944662fa2485b45ce8cb8e5c2
https://doi.org/10.1016/0003-9861(88)90345-1

Zobrazit plný text záznamu

Active-Site Heterogeneity as Revealed by Peroxide and Mercury: Interactions with Purified Subunits of Limulus Hemocyanin

Autor: Richard W. Topham, Celia Bonaventura, Shirley Tesh, Joseph Bonaventura

Publikováno v: Invertebrate Oxygen Carriers ISBN: 9783540169437

Previous work has shown that the active sites of mollusc and arthropod hemocyanins may be differentiated by their interactions with hydrogen peroxide and with mercury. In contrast to mollusc hemocyanins, the arthropod hemocyanins are typically oxidiz

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7159e598d267e49e42d55576f92c37f8
https://doi.org/10.1007/978-3-642-71481-8_68

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání