F
Francesco Malatesta
Researcher at University of L'Aquila
Publications - 53
Citations - 1404
Francesco Malatesta is an academic researcher from University of L'Aquila. The author has contributed to research in topics: Cytochrome c oxidase & Cytochrome c. The author has an hindex of 19, co-authored 53 publications receiving 1357 citations. Previous affiliations of Francesco Malatesta include University of Rome Tor Vergata.
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Journal ArticleDOI
The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis
Giuliano Sciara,Steven G. Kendrew,Adriana E. Miele,Neil G. Marsh,Luca Federici,Francesco Malatesta,Giuliana Schimperna,Carmelinda Savino,Beatrice Vallone +8 more
TL;DR: This is the first crystal structure of an enzyme involved in the tailoring of a type II aromatic polyketide and illustrates some of the enzyme–substrate recognition features that may apply to a range of other enzymes involved in modifying apolyketide core structure.
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Structure and function of a molecular machine: cytochrome c oxidase.
TL;DR: This review presents and discusses some of the relevant spectroscopic and kinetic properties of the prosthetic groups of cytochrome c oxidase.
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Tryptophan 121 of Subunit II Is the Electron Entry Site to Cytochrome-c Oxidase in Paracoccus denitrificans INVOLVEMENT OF A HYDROPHOBIC PATCH IN THE DOCKING REACTION
TL;DR: 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.
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Cytochrome-c oxidase. Subunit structure and proton pumping.
TL;DR: The significance of the subunit structure of cytochrome-c oxidase in proton pumping is reviewed and available evidences for or against a role of subunit III in the control of this important function of the enzyme are summarized.
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Interaction of cytochrome c with cytochrome oxidase: two different docking scenarios.
TL;DR: Recent results obtained from bacterial cytochrome c oxidases from both Paracoccus denitrificans, in which the primary electrostatic encounter most closely matches the mitochondrial situation, and the Thermus thermophilus ba(3) oxidase in which docking and electron transfer is predominantly based on hydrophobic interactions.