Protein dynamics. Comparative investigation on heme-proteins with different physiological roles

Autor: Maurizio Leone, Enrico Gratton, E. Vitrano, E. E. Di Iorio, L. Cordone, Kaspar H. Winterhalter, Antonio Cupane, D. Filipovic, U.R. Hiltpold

Publikováno v: DILORIO, EE; HILTPOLD, UR; FILIPOVIC, D; WINTERHALTER, KH; GRATTON, E; VITRANO, E; et al.(1991). PROTEIN DYNAMICS-COMPARATIVE INVESTIGATION ON HEME-PROTEINS WITH DIFFERENT PHYSIOLOGICAL ROLES. BIOPHYSICAL JOURNAL, 59(3), 742-754. doi: 10.1016/S0006-3495(91)82287-1. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/7c71x3bn
Scopus-Elsevier

We report the low temperature carbon monoxide recombination kinetics after photolysis and the temperature dependence of the visible absorption spectra of the isolated alpha SH-CO and beta SH-CO subunits from human hemoglobin A in ethylene glycol/wate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c452ee67df1b1ab15442536bc9c4502e
https://doi.org/10.1016/s0006-3495(91)82287-1

Crystal structure of Asian elephant (Elephas maximus) cyano-metmyoglobin at 1.78-A resolution. Phe29(B10) accounts for its unusual ligand binding properties

Autor: D A, Bisig, E E, Di Iorio, K, Diederichs, K H, Winterhalter, K, Piontek

Publikováno v: The Journal of biological chemistry. 270(35)

The crystal structure of Asian elephant cyano-metmyoglobin which has a glutamine instead of the usual distal site histidine has been determined to high resolution. In addition to this replacement, the substitution of a conserved leucine residue in po

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e9967a3585b0273852bd30c91a8de8da
https://pubmed.ncbi.nlm.nih.gov/7657658

Protein dynamics in minimyoglobin: is the central core of myoglobin the conformational domain?

Autor: G. De Sanctis, Kaspar H. Winterhalter, B. Giardina, Weiming Yu, E. E. Di Iorio, F. Ascoli, G. Falcioni, M. Brunori, C. Calonder

Publikováno v: Scopus-Elsevier

The kinetics of CO binding to the horse myoglobin fragment Mb-(32-139), the so-called "mini-Mb," were investigated by laser flash photolysis in 0.1 M phosphate buffer and in buffer with 75% (vol/vol) glycerol. The reaction displays complex time cours

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63c5a18cb69d8453a80c1718422ce918
http://hdl.handle.net/11581/243087

The reaction of hemoglobin Zürich with oxygen and carbon monoxide

Autor: Eraldo Antonini, Gm Giacometti, Maurizio Brunori, E. E. Di Iorio, Kaspar H. Winterhalter

Publikováno v: Journal of Biological Chemistry. 255:6160-6165

The present paper reports a spectroscopic and kinetic study of the reaction with oxygen and carbon monoxide of (a) the abnormal hemoglobin Zurich (beta 63, E7 His leads to Arg), (b) its isolated abnormal chains (beta ZH), and (c) a reconstituted hybr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f6b8c1ae4f7a3853f9fbb7db99bb03dc
https://doi.org/10.1016/s0021-9258(18)43715-5

Kinetics of carbon monoxide binding to phenobarbital-induced cytochrome P-450 from rat liver microsomes: a simple bimolecular process

Autor: Kaspar H. Winterhalter, E. E. Di Iorio, Maja Oertle, Christoph Richter

Publikováno v: Proceedings of the National Academy of Sciences. 82:4900-4904

The kinetics of carbon monoxide binding to phenobarbital-induced cytochrome P-450 (P-450PB) and to its enzymatically inactive form P-420PB have been investigated by both stopped-flow and flash-photolysis spectrophotometry. When the simultaneous prese

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7486c285489e825e80c9cfb2eacd7317
https://doi.org/10.1073/pnas.82.15.4900