Interactions between Phospholipids and NADH:Ubiquinone Oxidoreductase (Complex I) from Bovine Mitochondria

Autor: Judy Hirst, Mark S. Sharpley, Richard J. Shannon, Federica Draghi

Publikováno v: Biochemistry. 45:241-248

NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria is a highly complicated, energy transducing, membrane-bound enzyme. It contains 46 different subunits and nine redox cofactors: a noncovalently bound flavin mononucleotide and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99aa6fc4126159cc0b8486d6b33dd7b4
https://doi.org/10.1021/bi051809x

The carbon monoxide derivative of human hemoglobin carrying the double mutation LeuB10→Tyr and HisE7→Gln on α and β chains probed by infrared spectroscopy

Autor: Adriana E. Miele, Beatrice Vallone, Federica Draghi, Alberto Boffi

Publikováno v: Archives of Biochemistry and Biophysics. 402:59-64

The fine structural properties of the distal heme pocket have been probed by infrared spectroscopy of ferrous carbon monoxy human hemoglobin mutants carrying the mutations LeuB10-->Tyr and HisE7-->Gln on the alpha, beta, and both chains, respectively

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64c8b5ac96eff32aaae5f75d78ccfa49
https://doi.org/10.1016/s0003-9861(02)00061-9

Control of Heme Reactivity by Diffusion: Structural Basis and Functional Characterization in Hemoglobin Mutants

Autor: Maurizio Brunori, Beatrice Vallone, Carlo Travaglini-Allocatelli, Alessandro Arcovito, Adriana E. Miele, Andrea Bellelli, Federica Draghi

Publikováno v: Biochemistry. 40:14449-14458

The effect of mutagenesis on O(2), CO, and NO binding to mutants of human hemoglobin, designed to modify some features of the reactivity that hinder use of hemoglobin solutions as blood substitute, has been extensively investigated. The kinetics may

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e3add643942fd5d8e0eeed5e404f6de
https://doi.org/10.1021/bi011602d

Pattern of cavities in globins: the case of human hemoglobin

Autor: Kenneth A. Johnson, Carmelinda Savino, Federica Draghi, Adriana E. Miele, Giuliano Sciara, Beatrice Vallone, Maurizio Brunori

Publikováno v: Biopolymers
Biopolymers, Wiley, 2009, 91 (12), pp.1097-1107. ⟨10.1002/bip.21201⟩
91 (2009): 1097–1107. doi:10.1002/bip.21201
info:cnr-pdr/source/autori:Savino C; Miele, A.E.; Draghi F.; Johnson K.A.; Sciara G.; Brunori M.; Vallone B./titolo:Pattern of cavities in globins: The case of human hemoglobin./doi:10.1002%2Fbip.21201/rivista:Biopolymers (Print)/anno:2009/pagina_da:1097/pagina_a:1107/intervallo_pagine:1097–1107/volume:91

In this paper we used the technique of filling with xenon atoms the hydrophobic cavities, previously referred to as packing defects, naturally present in myoglobin and hemoglobin. Our aim is to demonstrate up to which point the primary sequence is re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64985b65fcdae4daae87827508e2ee26
https://pubmed.ncbi.nlm.nih.gov/19365817

Controlling ligand binding in myoglobin by mutagenesis

Autor: John S. Olson, Federica Draghi, Beatrice Vallone, Adriana E. Miele, Carlo Travaglini-Allocatelli, Quentin H. Gibson, Maurizio Brunori

Publikováno v: The Journal of biological chemistry. 277(9)

A quadruple mutant of sperm whale myoglobin was constructed to mimic the structure found in Ascaris suum hemoglobin. The replacements include His(E7)--Gln, Leu(B10)--Tyr, Thr(E10)--Arg, and Ile(G8)--Phe. Single, double, and triple mutants were charac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31f3359fb84a3075f7e12cca7654351f
https://pubmed.ncbi.nlm.nih.gov/11744723