Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Benet C. Prickril"'
Autor:
Donald M. Kurtz, Eric D. Coulter, Zanna M. Beharry, Neeta V. Shenvi, Benet C. Prickril, Jennifer J. Smith
Publikováno v:
Inorganica Chimica Acta. 297:231-241
Investigations were undertaken aimed at distinguishing and clarifying the reactivities of the Fe(SCys) 4 and diironoxo sites of rubrerythrin (Rr) during its catalysis of substrate oxidations by either dioxygen or hydrogen peroxide. Three Rr-cataly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b1ff7a792b458e8f30c8a2f9b899958e
https://doi.org/10.1016/s0020-1693(99)00374-6
https://doi.org/10.1016/s0020-1693(99)00374-6
Autor:
Benet C. Prickril, Donald M. Kurtz
Publikováno v:
Biochemical and Biophysical Research Communications. 181:337-341
Two regions in the amino acid sequence of the 21.5 kDa subunit of rubrerythrin from Desulfovibrio vulgaris (Hildenborough) are shown to be homologous. Rubrerythrin contains a non-heme, non-sulfur diiron site, and the internally homologous regions sha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36ba9bf0fb749fd6bcc93d8c32a68ba4
https://doi.org/10.1016/s0006-291x(05)81423-8
https://doi.org/10.1016/s0006-291x(05)81423-8
Publikováno v:
Biochemistry. 30:11118-11123
The gene coding for rubrerythrin from the sulfate-reducing bacterium Desulfovibrio vulgaris (Hildenborough) has been cloned and sequenced. Rubrerythrin is known to contain two types of iron sites: one rubredoxin-like FeS4 center in each of the two id
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9398c6fea857c1129c93bdc5a8149785
https://doi.org/10.1021/bi00110a014
https://doi.org/10.1021/bi00110a014
Publikováno v:
Biochemistry. 33(12)
Resonance Raman (RR) spectra of the non-heme iron protein rubrerythrin from Desulfovibrio vulgaris unequivocally demonstrate the presence of both a rubredoxin-type FeS4 site and a (mu-oxo)diiron(III) cluster. The RR spectra of rubrerythrin excited at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b2d5e2563768d217b28b411200e0c75
https://pubmed.ncbi.nlm.nih.gov/8142354
https://pubmed.ncbi.nlm.nih.gov/8142354
Publikováno v:
Biochemistry. 32(33)
Rubrerythrin, a contraction of rubredoxin and hemerythrin, is the trivial name given to a non-heme iron protein isolated from Desulfovibrio vulgaris (Hildenborough). This protein, whose physiological function is unknown, was first characterized by J.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aad4a3e40385cd090e03671c7ee8229f
https://pubmed.ncbi.nlm.nih.gov/8395205
https://pubmed.ncbi.nlm.nih.gov/8395205
Autor:
Francesco Bonomi, Benet C. Prickril, B.H. Huynh, Natarajan Ravi, Nishi Gupta, Donald M. Kurtz
Publikováno v:
Journal of Inorganic Biochemistry. 51:508
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e9ea8669751755220e2edfc97e0084ca
https://doi.org/10.1016/0162-0134(93)85536-h
https://doi.org/10.1016/0162-0134(93)85536-h
Autor:
Benet C. Prickril, Boi H. Huynh, Guy Fauque, Daniel V. DerVartanian, Alan Przybyla, Isabel Moura, Eui-Sung Choi, Shao-Hua He, Miguel Teixeira, Harry D. Peck, Jean LeGall, Ching Li, José J. G. Moura, Nanda K. Menon, D.S. Patil
Publikováno v:
Biochemical and biophysical research communications. 149(2)
A comparison of amino-terminal amino acid sequences from the large and small subunits of hydrogenases from Desulfovibrio reveals significant differences. These results, in conjunction with antibody analyses, clearly indicate that the iron, iron + nic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a96f77afe5595e56cf947172c2444d2
https://pubmed.ncbi.nlm.nih.gov/3322275
https://pubmed.ncbi.nlm.nih.gov/3322275
Autor:
Jean LeGall, Benet C. Prickril, Boi Hanh Huynh, Isabel Moura, António V. Xavier, José J. G. Moura
Publikováno v:
Biochemistry. 27(5)
A new non-heme iron protein from the periplasmic fraction of Desulfovibrio vulgaris (Hildenbourough NCIB 8303) has been purified to homogeneity, and its amino acid composition, molecular weight, redox potential, iron content, and optical, EPR, and Mo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebb9200c5e77fe5909d7d3d3c0c41f20
https://pubmed.ncbi.nlm.nih.gov/2835096
https://pubmed.ncbi.nlm.nih.gov/2835096
Autor:
Jean LeGall, Harry D. Peck, Miguel Teixeira, B.H. Huynh, José J. G. Moura, Isabel Moura, Benet C. Prickril, Melvin H. Czechowski, Daniel V. DerVartanian, D.S. Patil
Publikováno v:
Universidade Nova de Lisboa
CIÊNCIAVITAE
CIÊNCIAVITAE
The [NiFe] hydrogenase isolated from Desulfovibrio gigas was poised at different redox potentials and studied by Mossbauer spectroscopy. The data firmly establish that this hydrogenase contains four prosthetic groups: one nickel center, one [3Fe-xS],
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::031e3f595dccbf63b7c86358a3852dd8
https://novaresearch.unl.pt/en/publications/5cc57ce7-93b9-42b4-beda-55986f4ef47e
https://novaresearch.unl.pt/en/publications/5cc57ce7-93b9-42b4-beda-55986f4ef47e
Autor:
Daniel V. DerVartanian, José J. G. Moura, Marly K. Eidsness, Isabel Moura, Jean LeGall, Benet C. Prickril, Harry D. Peck, Robert A. Scott
Publikováno v:
Ciência Vitae
Scopus-Elsevier
Scopus-Elsevier
Ni and Se x-ray absorption spectroscopic studies of the [NiFeSe]hydrogenases from Desulfovibrio baculatus are described. The Ni site geometry is pseudo-octahedral with a coordinating ligand composition of 3-4 (N,O) at 2.06 A, 1-2 (S,Cl) at 2.17 A, an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3eb70068f09d52ffecd7ac429b1372c
http://www.scopus.com/inward/record.url?eid=2-s2.0-0024485986&partnerID=MN8TOARS
http://www.scopus.com/inward/record.url?eid=2-s2.0-0024485986&partnerID=MN8TOARS