• Publications
  • Influence
Neuroglobin, nitric oxide, and oxygen: functional pathways and conformational changes.
Based on the ligand-linked conformational changes discovered by crystallography, the pathways of the reactions with O2 and NO provide a framework that may account for the involvement of Ngb in controlling the activation of a protective signaling mechanism. Expand
A Novel Type of Nitric-oxide Reductase
A novel family of prokaryotic NO reductases, with a non-heme di-iron site as the catalytic center, was established, and was shown that the activity was due to the A-type flavoprotein core, as the rubredoxin domain alone exhibited no activity. Expand
The structure of the endoribonuclease XendoU: From small nucleolar RNA processing to severe acute respiratory syndrome coronavirus replication
The conserved structural determinants of this site may provide a framework for attempting to design antiviral drugs to interfere with the infectious nidovirus life cycle. Expand
Molecular adaptation to physiological requirements: the hemoglobin system of trout.
  • M. Brunori
  • Biology, Medicine
  • Current topics in cellular regulation
  • 1975
On the basis of the behavior of the isolated hemoglobin components from trout blood and of their distribution among the erythrocytes, it has been possible to provide a “rationale” for the existence of several hemoglobins. Expand
Complex landscape of protein structural dynamics unveiled by nanosecond Laue crystallography
It is proposed that the extended relaxation of the globin moiety reflects reequilibration among conformational substates known to play an essential role in controlling protein function. Expand
Tryptophan 121 of Subunit II Is the Electron Entry Site to Cytochrome-c Oxidase in Paracoccus denitrificans
There is evidence that Trp-121 which is surrounded by a hydrophobic patch is the electron entry site to oxidase, and it is proposed that this patch is required for a fine tuning of the redox partners in the initial collisional complex to obtain a configuration optimal for electron transfer. Expand
NO sensing in Pseudomonas aeruginosa: structure of the transcriptional regulator DNR.
This is the first structure of a putative NO-sensing bacterial transcriptional regulator and reveals the presence of a large hydrophobic cavity that may be the cofactor binding site in apo-DNR, supporting the hypothesis that NO sensing involves gas binding to the ferrous heme. Expand
Studies on the functional properties of fish hemoglobins. II. The oxygen equilibrium of the isolated hemoglobin components from trout blood.
The different oxygen-binding behavior of the isolated components can explain data obtained with the whole blood and in particular the contribution of the various proteins to the Root effect. Expand
Cavities and packing defects in the structural dynamics of myoglobin
Results convey the general picture that pre‐existing internal cavities are involved in controlling the dynamics and reactivity of the reactions of Mb with O2 and other ligands, including NO. Expand